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词条 Affimer
释义

  1. Development

  2. Production

  3. Properties

  4. Applications

      Reagents and Diagnostics    Therapeutics  

  5. References

  6. External links

Affimer molecules[1] are small proteins that bind to target molecules with similar specificity and affinity to that of antibodies.[2][3] These engineered non-antibody binding proteins are designed to mimic the molecular recognition characteristics of monoclonal antibodies in different applications.[2][4] In addition, these affinity reagents have been optimized to increase their stability,[5] make them tolerant to a range of temperatures and pH,[6] reduce their size, and to increase their expression in E.coli and mammalian cells.[2]

Development

Affimer proteins were developed initially at the MRC Cancer Cell Unit in Cambridge then across two laboratories at the University of Leeds.[7][8][9][10] Derived from the cysteine protease inhibitor family of cystatins, which function in nature as cysteine protease inhibitors,[11][12] these 12–14 kDa proteins share the common tertiary structure of an alpha-helix lying on top of an anti-parallel beta-sheet.[13]

Affimer proteins display two peptide loops and an N-terminal sequence that can all be randomised to bind to desired target proteins with high affinity and specificity,[5] in a similar manner to monoclonal antibodies. Stabilisation of the two peptides by the protein scaffold constrains the possible conformations that the peptides can take, increasing the binding affinity and specificity compared to libraries of free peptides.

Production

Phage display libraries of 1010 randomised potential target interaction sequences[14] are used to screen for Affimer proteins that exhibit high-specificity binding to the target protein with binding affinities in the nM range.[5][15][16] The ability to direct in vitro screening techniques allows the identification of highly specific, high affinity Affimer binders, negating requirements for affinity maturation of these reagents. In vitro screening and development also mean that the target space for Affimer binders is not limited by an animal host’s immune system. Due to Affimer proteins being generated using recombinant systems, their generation is significantly more rapid and reproducible compared to the production of traditional antibodies.[17]

Multimeric forms of Affimer proteins have been generated and shown to yield titrimetric volumes in the range of 200–400 mg/L under small scale culture using bacterial host systems. Multimeric forms of Affimer proteins with the same target specificity provided avidity effects in target binding, while fusion of different Affimer proteins with different target specificities would enable multi-specific affinity proteins.[18]

Many different tags and fusion proteins, such as fluorophores, single-stranded DNA, His, and c-Myc tags can be easily conjugated to Affimer proteins.[2][19][20][21][22][23] Specific cysteine residues can be introduced to the protein to allow thiol chemistry to uniformly orient Affimer proteins on a solid support for the purposes of increasing target capture in ligand binding assays and biosensors.[5][15][17][24][25] This flexible functionalisation of the Affimer molecule maximises the performance of Affimer reagents across multiple applications and assay formats.

Properties

Affimer binders are recombinant proteins. They display the robust characteristics of high thermostability, with melting temperatures over 80 °C,[10] resistance to extremes of pH (2–13.7),[10] freeze-thaw cycles and lyophilisation. The low molecular weight of Affimer binders means that problems of steric hindrance, that are typically observed with antibodies, may be avoided.[2] As they are manufactured using recombinant bacterial production processes, the batch-to-batch consistency is maintained for Affimer reagents, overcoming some of the issues of reproducibility and security of supply.[2][3][17][26][27]

These synthetic antibodies were engineered to be stable, non-toxic, biologically neutral and contain no post-translational modifications or disulfide bridges.[7][8][10] Two separate loop sequences, incorporating a total of 12 to 36 amino acids, form the target interaction surface so interaction surfaces can range form 650–1000 Å. The large interaction surface is purported to result in highly-specific, high affinity binding to target proteins.[5][7][10][15][17][19][28][29][30][31] As a result, Affimer molecules can distinguish between proteins that differ by only a single amino acid, can detect subtle changes in protein expression levels even in a multiplexed format and can distinguish between multiple closely related protein domains.[2][24][31][32][33]

Applications

Affimer technology has been commercialised and developed by Avacta, who are developing these affinity reagents as tools for research and diagnostics and as biotherapeutics.

Reagents and Diagnostics

Affimer binders have been used across a number of platforms, including ELISA,[2][17][34] surface plasmon resonance,[32][34][35][36] affinity purification,[2][34][37] immunohistochemistry[2] and immunocytochemistry, including super resolution imaging.[2][19][20][21] Affimer reagents that inhibit protein-protein interactions can also be produced with the potential to express these inhibitors in mammalian cells to investigate and modify signalling pathways.[2][32][35][38][39] They have also been co-crystallised in complex with target proteins,[32][35][40] enabling drug discovery through in silico screening and displacement assays.[14]

Affimer reagents are suitable for use in biosensors,[5][15][24][25] point-of-care diagnostics and as anti-idiotypic reagents in pharmacokinetic and therapeutic drug monitoring assays.[26][27][31][41][42]

Therapeutics

The Affimer protein scaffold has been developed as a biotherapeutic. The small size and stability profile of Affimer proteins combined with their human origin confer drug-like properties to Affimer molecules. This may represent advantages over antibodies in terms of tissue penetration, for example in solid tumours or for non-invasive topical administration, such as inhaled delivery or dermal application.[18]

Affimer proteins can be easily conjugated to form mutlimers and be easily functionalised for the design of therapeutics with specific desired characteristics. Examples include the production of multi-specific Affimer molecules to target and recruit specific cells, fusion to Fc fragments or albumin binders to tune their half-life in vivo and for use as the targeting moiety in chimeric receptors or modified to carry a toxin in Affimer-drug conjugates.[16][18][43]

Affimer therapeutics are in discovery and preclinical development to tackle blood clotting disorders, antibiotic resistance, phenotypic drug discovery models and cancer, both via CAR-T cell therapy and as immune checkpoint inhibitors.[18][44][45][46] Early studies using ex vivo human samples showed low immunogenicity associated with the Affimer scaffold, at levels comparable to a marketed antibody therapeutic.[47] Furthermore, initial preclinical studies showed good efficacy and tolerability of the anti-PDL1 immuno-oncology Affimer therapeutic in mice. It is anticipated that IND filiing for the first Affimer therapeutic will occur in 2019/2020.[16][48]

References

1. ^Proprietary name, owned by Avacta
2. ^1 2 3 4 5 6 7 8 9 10 11 {{cite journal | vauthors = Tiede C, Bedford R, Heseltine SJ, Smith G, Wijetunga I, Ross R, AlQallaf D, Roberts AP, Balls A, Curd A, Hughes RE, Martin H, Needham SR, Zanetti-Domingues LC, Sadigh Y, Peacock TP, Tang AA, Gibson N, Kyle H, Platt GW, Ingram N, Taylor T, Coletta LP, Manfield I, Knowles M, Bell S, Esteves F, Maqbool A, Prasad RK, Drinkhill M, Bon RS, Patel V, Goodchild SA, Martin-Fernandez M, Owens RJ, Nettleship JE, Webb ME, Harrison M, Lippiat JD, Ponnambalam S, Peckham M, Smith A, Ferrigno PK, Johnson M, McPherson MJ, Tomlinson DC | display-authors = 6 | title = Affimer proteins are versatile and renewable affinity reagents | journal = eLife | volume = 6 | date = June 2017 | pmid = 28654419 | pmc = 5487212 | doi = 10.7554/elife.24903 }}
3. ^1 {{cite journal | vauthors = Klont F, Hadderingh M, Horvatovich P, Ten Hacken NH, Bischoff R | title = Affimers as an Alternative to Antibodies in an Affinity LC-MS Assay for Quantification of the Soluble Receptor of Advanced Glycation End-Products (sRAGE) in Human Serum | journal = Journal of Proteome Research | volume = 17 | issue = 8 | pages = 2892–2899 | date = August 2018 | pmid = 30005571 | pmc = 6079930 | doi = 10.1021/acs.jproteome.8b00414 }}
4. ^{{Cite web|url=https://www.the-scientist.com/features/antibody-alternatives-34125|title=Antibody Alternatives|website=The Scientist Magazine® | access-date=2018-10-18}}
5. ^1 2 3 4 5 {{cite journal | vauthors = Sharma R, Deacon SE, Nowak D, George SE, Szymonik MP, Tang AA, Tomlinson DC, Davies AG, McPherson MJ, Wälti C | title = Label-free electrochemical impedance biosensor to detect human interleukin-8 in serum with sub-pg/ml sensitivity | journal = Biosensors & Bioelectronics | volume = 80 | pages = 607–613 | date = June 2016 | pmid = 26897263 | pmc = 4785862 | doi = 10.1016/j.bios.2016.02.028 }}
6. ^{{cite journal | vauthors = Rawlings AE, Bramble JP, Tang AA, Somner LA, Monnington AE, Cooke DJ, McPherson MJ, Tomlinson DC, Staniland SS | title = Phage display selected magnetite interacting Adhirons for shape controlled nanoparticle synthesis | journal = Chemical Science | volume = 6 | issue = 10 | pages = 5586–5594 | date = October 2015 | pmid = 29861896 | pmc = 5949846 | doi = 10.1039/C5SC01472G }}
7. ^1 2 {{cite journal | vauthors = Woodman R, Yeh JT, Laurenson S, Ko Ferrigno P | title = Design and validation of a neutral protein scaffold for the presentation of peptide aptamers | journal = Journal of Molecular Biology | volume = 352 | issue = 5 | pages = 1118–33 | date = October 2005 | pmid = 16139842 | doi = 10.1016/j.jmb.2005.08.001 }}
8. ^1 {{cite journal | vauthors = Hoffmann T, Stadler LK, Busby M, Song Q, Buxton AT, Wagner SD, Davis JJ, Ko Ferrigno P | title = Structure-function studies of an engineered scaffold protein derived from stefin A. I: Development of the SQM variant | journal = Protein Engineering, Design & Selection | volume = 23 | issue = 5 | pages = 403–13 | date = May 2010 | pmid = 20179045 | pmc = 2851446 | doi = 10.1093/protein/gzq012 }}
9. ^{{cite journal | vauthors = Stadler LK, Hoffmann T, Tomlinson DC, Song Q, Lee T, Busby M, Nyathi Y, Gendra E, Tiede C, Flanagan K, Cockell SJ, Wipat A, Harwood C, Wagner SD, Knowles MA, Davis JJ, Keegan N, Ferrigno PK | title = Structure-function studies of an engineered scaffold protein derived from Stefin A. II: Development and applications of the SQT variant | journal = Protein Engineering, Design & Selection | volume = 24 | issue = 9 | pages = 751–63 | date = September 2011 | pmid = 21616931 | doi = 10.1093/protein/gzr019 }}
10. ^1 2 3 4 {{cite journal | vauthors = Tiede C, Tang AA, Deacon SE, Mandal U, Nettleship JE, Owen RL, George SE, Harrison DJ, Owens RJ, Tomlinson DC, McPherson MJ | title = Adhiron: a stable and versatile peptide display scaffold for molecular recognition applications | journal = Protein Engineering, Design & Selection | volume = 27 | issue = 5 | pages = 145–55 | date = May 2014 | pmid = 24668773 | pmc = 4000234 | doi = 10.1093/protein/gzu007 }}
11. ^{{cite journal | vauthors = Turk V, Stoka V, Turk D | title = Cystatins: biochemical and structural properties, and medical relevance | journal = Frontiers in Bioscience | volume = 13 | issue = 13 | pages = 5406–20 | date = May 2008 | pmid = 18508595 | doi = 10.2741/3089 }}
12. ^{{cite journal | vauthors = Kondo H, Abe K, Emori Y, Arai S | title = Gene organization of oryzacystatin-II, a new cystatin superfamily member of plant origin, is closely related to that of oryzacystatin-I but different from those of animal cystatins | journal = FEBS Letters | volume = 278 | issue = 1 | pages = 87–90 | date = January 1991 | pmid = 1993479 | doi = 10.1016/0014-5793(91)80090-p }}
13. ^{{cite journal | vauthors = Turk V, Bode W | title = The cystatins: protein inhibitors of cysteine proteinases | journal = FEBS Letters | volume = 285 | issue = 2 | pages = 213–9 | date = July 1991 | pmid = 1855589 | doi = 10.1016/0014-5793(91)80804-C }}
14. ^1 {{cite journal | vauthors = Arrata I, Barnard A, Tomlinson DC, Wilson AJ | title = Interfacing native and non-native peptides: using Affimers to recognise α-helix mimicking foldamers | journal = Chemical Communications | volume = 53 | issue = 19 | pages = 2834–2837 | date = March 2017 | pmid = 28217789 | doi = 10.1039/c6cc09395g }}
15. ^1 2 3 {{cite journal | vauthors = Zhurauski P, Arya SK, Jolly P, Tiede C, Tomlinson DC, Ko Ferrigno P, Estrela P | title = Sensitive and selective Affimer-functionalised interdigitated electrode-based capacitive biosensor for Her4 protein tumour biomarker detection | journal = Biosensors & Bioelectronics | volume = 108 | pages = 1–8 | date = June 2018 | pmid = 29482002 | doi = 10.1016/j.bios.2018.02.041 }}
16. ^1 2 {{Cite journal|last=Basran|first=Amrik|last2=Stanley|first2=Emma | name-list-format = vanc |date=2018-07-01|title=Abstract 3776: Generation and formatting of an Affimer® biotherapeutic for the inhibition of the PD-L1/PD-1 pathway: Proof of concept in mouse|url=http://cancerres.aacrjournals.org/content/78/13_Supplement/3776|journal=Cancer Research | volume=78|issue=13 Supplement|pages=3776|doi=10.1158/1538-7445.AM2018-3776|issn=0008-5472}}
17. ^1 2 3 4 {{cite journal | vauthors = Xie C, Tiede C, Zhang X, Wang C, Li Z, Xu X, McPherson MJ, Tomlinson DC, Xu W | title = Development of an Affimer-antibody combined immunological diagnosis kit for glypican-3 | journal = Scientific Reports | volume = 7 | issue = 1 | pages = 9608 | date = August 2017 | pmid = 28852111 | pmc = 5575301 | doi = 10.1038/s41598-017-10083-w }}
18. ^1 2 3 {{Cite journal|title=Interview with Amrik Basran at Avacta Life Sciences|url=https://www.drugtargetreview.com/article/11013/interview-amrik-basran-chief-scientific-officer-avacta-life-sciences/|journal=Drug Target Review }}
19. ^1 2 {{cite journal | vauthors = Schlichthaerle T, Eklund AS, Schueder F, Strauss MT, Tiede C, Curd A, Ries J, Peckham M, Tomlinson DC, Jungmann R | title = Site-Specific Labeling of Affimers for DNA-PAINT Microscopy | journal = Angewandte Chemie | volume = 57 | issue = 34 | pages = 11060–11063 | date = August 2018 | pmid = 29873161 | doi = 10.1002/anie.201804020 }}
20. ^1 {{cite journal | vauthors = Bedford R, Tiede C, Hughes R, Curd A, McPherson MJ, Peckham M, Tomlinson DC | title = Alternative reagents to antibodies in imaging applications | journal = Biophysical Reviews | volume = 9 | issue = 4 | pages = 299–308 | date = August 2017 | pmid = 28752365 | pmc = 5578921 | doi = 10.1007/s12551-017-0278-2 }}
21. ^1 {{cite journal | vauthors = Lopata A, Hughes R, Tiede C, Heissler SM, Sellers JR, Knight PJ, Tomlinson D, Peckham M | title = Affimer proteins for F-actin: novel affinity reagents that label F-actin in live and fixed cells | journal = Scientific Reports | volume = 8 | issue = 1 | pages = 6572 | date = April 2018 | pmid = 29700342 | pmc = 5920084 | doi = 10.1038/s41598-018-24953-4 }}
22. ^{{cite journal | vauthors = Wang W, Guo Y, Tiede C, Chen S, Kopytynski M, Kong Y, Kulak A, Tomlinson D, Chen R, McPherson M, Zhou D | title = Ultraefficient Cap-Exchange Protocol To Compact Biofunctional Quantum Dots for Sensitive Ratiometric Biosensing and Cell Imaging | journal = ACS Applied Materials & Interfaces | volume = 9 | issue = 18 | pages = 15232–15244 | date = May 2017 | pmid = 28421739 | pmc = 5432960 | doi = 10.1021/acsami.6b13807 }}
23. ^{{cite journal | vauthors = Fisher MJ, Williamson DJ, Burslem GM, Plante JP, Manfield IW, Tiede C, Ault JR, Stockley PG, Plein S, Maqbool A, Tomlinson DC, Foster R, Warriner SL, Bon RS | title = Trivalent Gd-DOTA reagents for modification of proteins | journal = RSC Advances | volume = 5 | issue = 116 | pages = 96194–96200 | date = December 2015 | pmid = 27019702 | pmc = 4786947 | doi = 10.1039/c5ra20359g }}
24. ^1 2 {{cite journal | vauthors = Weckman NE, McRae C, Ko Ferrigno P, Seshia AA | title = Comparison of the specificity and affinity of surface immobilised Affimer binders using the quartz crystal microbalance | journal = The Analyst | volume = 141 | issue = 22 | pages = 6278–6286 | date = October 2016 | pmid = 27704086 | doi = 10.1039/c6an01602b }}
25. ^1 {{cite journal | vauthors = Koutsoumpeli E, Tiede C, Murray J, Tang A, Bon RS, Tomlinson DC, Johnson S | title = Antibody Mimetics for the Detection of Small Organic Compounds Using a Quartz Crystal Microbalance | journal = Analytical Chemistry | volume = 89 | issue = 5 | pages = 3051–3058 | date = March 2017 | pmid = 28192970 | doi = 10.1021/acs.analchem.6b04790 }}
26. ^1 {{Cite web|url=https://www.avacta.com/resources/anti-idiotypic-binders-trastuzumab-validated-regulatory-bioanalysis-assay-collaboration|title=Anti-idiotypic binders for Trastuzumab validated in regulatory bioanalysis assay in collaboration with Covance | work = Avacta | access-date=2018-10-19}}
27. ^1 {{Cite web|url=https://www.avacta.com/resources/development-and-validation-anti-idiotypic-affmers-trastuzumab-pharmacokinetic-assay|title=Development and validation of anti-idiotypic Affmers to trastuzumab in a pharmacokinetic assay {{!}} Avacta|website=www.avacta.com | access-date=2018-10-19}}
28. ^{{cite journal | vauthors = Davis JJ, Tkac J, Laurenson S, Ko Ferrigno P | title = Peptide aptamers in label-free protein detection: 1. Characterization of the immobilized scaffold | journal = Analytical Chemistry | volume = 79 | issue = 3 | pages = 1089–96 | date = February 2007 | pmid = 17263340 | doi = 10.1021/ac061863z }}
29. ^{{cite journal | vauthors = Davis JJ, Tkac J, Humphreys R, Buxton AT, Lee TA, Ko Ferrigno P | title = Peptide aptamers in label-free protein detection: 2. Chemical optimization and detection of distinct protein isoforms | journal = Analytical Chemistry | volume = 81 | issue = 9 | pages = 3314–20 | date = May 2009 | pmid = 19320493 | doi = 10.1021/ac802513n }}
30. ^{{Cite web|url=https://www.avacta.com/resources/affimer-binders-improve-diagnostic-assay-performance-cdifficile-detection|title=Affimer binders improve diagnostic assay performance for C.difficile detection | work = Avacta | access-date=2018-10-19}}
31. ^1 2 {{Cite web|url=https://www.avacta.com/resources/development-and-characterisation-affimer-binders-4-leading-therapeutic-antibodies|title=Development and characterisation of Affimer binders to 4 leading therapeutic antibodies {{!}} Avacta|website=www.avacta.com | access-date=2018-10-19}}
32. ^1 2 3 {{cite journal | vauthors = Robinson JI, Baxter EW, Owen RL, Thomsen M, Tomlinson DC, Waterhouse MP, Win SJ, Nettleship JE, Tiede C, Foster RJ, Owens RJ, Fishwick CW, Harris SA, Goldman A, McPherson MJ, Morgan AW | title = Affimer proteins inhibit immune complex binding to FcγRIIIa with high specificity through competitive and allosteric modes of action | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 115 | issue = 1 | pages = E72-E81 | date = January 2018 | pmid = 29247053 | pmc = 5776790 | doi = 10.1073/pnas.1707856115 }}
33. ^{{cite journal | vauthors = Evans D, Johnson S, Laurenson S, Davies AG, Ko Ferrigno P, Wälti C | title = Electrical protein detection in cell lysates using high-density peptide-aptamer microarrays | journal = Journal of Biology | volume = 7 | issue = 1 | pages = 3 | date = 2008 | pmid = 18237447 | pmc = 2246035 | doi = 10.1186/jbiol62 }}
34. ^1 2 {{Cite web|url=https://www.avacta.com/resources/avacta-scientist-dr-geoff-platt-presents-affimer-data-webinar|title=Avacta Scientist Dr Geoff Platt presents Affimer data in webinar {{!}} Avacta|website=www.avacta.com|language=en|access-date=2018-10-22}}
35. ^1 2 {{cite journal | vauthors = Michel MA, Swatek KN, Hospenthal MK, Komander D | title = Ubiquitin Linkage-Specific Affimers Reveal Insights into K6-Linked Ubiquitin Signaling | journal = Molecular Cell | volume = 68 | issue = 1 | pages = 233–246.e5 | date = October 2017 | pmid = 28943312 | pmc = 5640506 | doi = 10.1016/j.molcel.2017.08.020 | url = https://linkinghub.elsevier.com/retrieve/pii/S1097276517306172 }}
36. ^{{cite journal | vauthors = Johnson A, Song Q, Ko Ferrigno P, Bueno PR, Davis JJ | title = Sensitive affimer and antibody based impedimetric label-free assays for C-reactive protein | language = EN | journal = Analytical Chemistry | volume = 84 | issue = 15 | pages = 6553–60 | date = August 2012 | pmid = 22789061 | doi = 10.1021/ac300835b }}
37. ^{{cite web |url= https://www.drugtargetreview.com/whitepaper/11094/affimer-reagents-facilitate-affinity-chromatography-purification-of-proteins/ |title=Affimer® reagents facilitate affinity chromatography purification |website=www.drugtargetreview.com |access-date=2018-10-22}}
38. ^{{cite journal | vauthors = Kyle HF, Wickson KF, Stott J, Burslem GM, Breeze AL, Tiede C, Tomlinson DC, Warriner SL, Nelson A, Wilson AJ, Edwards TA | title = Exploration of the HIF-1α/p300 interface using peptide and Adhiron phage display technologies | journal = Molecular BioSystems | volume = 11 | issue = 10 | pages = 2738–49 | date = October 2015 | pmid = 26135796 | doi = 10.1039/c5mb00284b }}
39. ^{{cite journal | vauthors = Heidelberger JB, Voigt A, Borisova ME, Petrosino G, Ruf S, Wagner SA, Beli P | title = Proteomic profiling of VCP substrates links VCP to K6-linked ubiquitylation and c-Myc function | journal = EMBO Reports | volume = 19 | issue = 4 | pages = e44754 | date = April 2018 | pmid = 29467282 | pmc = 5891417 | doi = 10.15252/embr.201744754 }}
40. ^{{cite journal | vauthors = Gersch M, Gladkova C, Schubert AF, Michel MA, Maslen S, Komander D | title = Mechanism and regulation of the Lys6-selective deubiquitinase USP30 | language = En | journal = Nature Structural & Molecular Biology | volume = 24 | issue = 11 | pages = 920–930 | date = November 2017 | pmid = 28945249 | pmc = 5757785 | doi = 10.1038/nsmb.3475 }}
41. ^{{Cite web|url=https://www.avacta.com/covance-webinar|title=Covance validate Affimers as critical PK assay reagents | publisher = Avacta |access-date=2018-10-22}}
42. ^{{Cite news|url=https://intellicyt.com/webinar-multiplexing-specificity-and-species-cross-reactivity-in-biologics-discovery/|title=Webinar: Multiplexing Specificity and Species Cross Reactivity in Biologics Discovery (On-Demand) - Intellicyt|work=Intellicyt|access-date=2018-10-22|language=en-US}}
43. ^{{Cite web|url=https://www.avacta.com/resources/tmac-affimer-drug-conjugates|title=TMAC Affimer Drug Conjugates | work = Avacta |access-date=2018-10-22}}
44. ^{{Cite news|url=http://sourcelifescience.com/source-clusters/item/16-avacta-and-memorial-sloan-kettering-cancer-center-in-cell-therapy-research-collaboration|title=Avacta and Memorial Sloan Kettering Cancer Center in cell therapy research collaboration|last=Mulligan|first=Tom|access-date=2018-10-22|language=en-gb}}
45. ^{{Cite web|url=https://www.avacta.com/therapeutics/pipeline|title=Pipeline {{!}} Avacta|website=www.avacta.com|language=en|access-date=2018-10-22}}
46. ^{{cite journal | vauthors = King R, Tiede C, Simmons K, Fishwick C, Tomlinson D, Ajjan R | title = Inhibition of complement C3 and fibrinogen interaction: a potential novel therapeutic target to reduce cardiovascular disease in diabetes | journal = Lancet | volume = 385 Suppl 1 | pages = S57 | date = February 2015 | pmid = 26312879 | doi = 10.1016/s0140-6736(15)60372-5 }}
47. ^{{Cite web|url=https://www.avacta.com/resources/affimer-technology-results-pbmc-immunogenicity-testing|title=Affimer Technology: Results of PBMC Immunogenicity Testing | work = Avacta |access-date=2018-10-22}}
48. ^{{Cite web|url=https://www.proactiveinvestors.co.uk/upload/SponsorFile/File/2018_04/1523004454_4---Avacta-.pdf|title=The Affimer Platform|last=Proactive Investors|first=|date=5 April 2018|website=Proactive Investors }}

External links

  • Avacta
  • [https://avacta.wistia.com/medias/xcwat7zy16 An Introduction to Affimer Technology - video]
{{Engineered antibodies}}

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