Rapid identification of Human Serum Albumin binding peptides from a phage display library:a back-of-the-envelope assessment of positive binders using titer-based criteria
- Published
- Accepted
- Subject Areas
- Biotechnology, Molecular Biology
- Keywords
- Binding peptide, Phage display technology, Quantitative criteria, Human serum albumin, Phage titers
- Copyright
- © 2015 Shi et al.
- Licence
- This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, reproduction and adaptation in any medium and for any purpose provided that it is properly attributed. For attribution, the original author(s), title, publication source (PeerJ PrePrints) and either DOI or URL of the article must be cited.
- Cite this article
- 2015. Rapid identification of Human Serum Albumin binding peptides from a phage display library:a back-of-the-envelope assessment of positive binders using titer-based criteria. PeerJ PrePrints 3:e1115v1 https://doi.org/10.7287/peerj.preprints.1115v1
Abstract
Human serum albumin (HSA) is the most abundant protein in blood and has a 19-day in vivo half-life, the longest human blood protein. HSA has also been extensively studied as a drug carrier in a wide variety of clinical applications. HSA-binding, compared with HSA-fusion, is promising strategy for extending the plasma half-life of protein therapeutics. The construction of albumin-binding drugs requires assessment of a large enough quantity of HSA-binding peptide candidates for conjugation with therapeutic proteins. Here, we report a back-of-the-envelope assessment method to facilitate phage display selection of HSA-binding peptides. With an experimentally determined number of phage titers, we can calculate the specificity ratios and the recovery yields. The recovery yield is calculated using the titers of eluted phage divided by the titers of input phage. The specificity ratio is calculated using the titer of eluted phage from a target-coated plate divided by the titer of eluted phage from a blank-control plate. These parameters are defined as quantitative criteria for panning and characterization of binding phage clones. Consequently, this approach may enable more rapid and low-cost phage display screening of HSA-binding peptides, which could be used as candidates of HSA binders for conjugation with therapeutic proteins.
Author Comment
This is a submission to PeerJ for review.