z-logo
Premium
Structure–Affinity Relationship Analysis and Affinity Maturation of a Calprotectin‐Binding Peptide
Author(s) -
FarreraSoler Lluc,
Hu CheWei,
Ricken Benjamin,
DíazPerlas Cristina,
Gerhold ChristianBenedikt,
Heinis Christian
Publication year - 2025
Publication title -
chembiochem
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.05
H-Index - 126
eISSN - 1439-7633
pISSN - 1439-4227
DOI - 10.1002/cbic.202500071
Peptide 3 is an 18‐amino acid linear peptide binding with sub‐micromolar affinity to the inflammation marker calprotectin. Its application in point‐of‐care diagnostic assays has shown promising results, yet improving its affinity for calprotectin could facilitate the development of sensitive and robust assays. Herein, a detailed structure–activity relationship analysis of Peptide 3 is reported to better understand the importance of each individual amino acid for the binding to calprotectin. Moreover, two different approaches have been followed here, one based on prolonging the peptide with random sequences and phage display selection, and one on screening chemically synthesized peptide variants containing non‐canonical amino acids, to increase its binding affinity. Combining several mutations that enhance affinity by small factors yielded Peptide 4 binding human calprotectin with a K D of 39 ± 5 nM measured by surface plasmon resonance spectroscopy, which is a five‐fold improvement compared to the previously reported Peptide 3.

This content is not available in your region!

Continue researching here.

Having issues? You can contact us here
Empowering knowledge with every search

Address

John Eccles House
Robert Robinson Avenue,
Oxford Science Park, Oxford
OX4 4GP, United Kingdom