In:
Molecular Systems Design & Engineering, Royal Society of Chemistry (RSC)
Abstract:
The sequence-to-function relationship of peptide-based catalysts remains a challenge, as even subtle modifications at the sequence level can alternate their catalytic activity. A set of linear and cyclic histidine-rich peptides was synthesized to assess the impact of amino acid disposition, cyclization, and incorporation of d -amino acids on their ability to self-assemble, coordinate Zn 2+ ions, and show intrinsic hydrolase-like activity. Self-assembly into β-sheets was confirmed for both linear peptides and one cyclic analogue (cy-hh) by FTIR, ThT binding, CD, and AFM. Interestingly, only peptide A demonstrated efficient ester hydrolysis of p -NPA, p -NPB and p -NPO substrates, indicative of its effective Zn 2+ coordination. Our findings highlight that increased rigidity of the peptide can hinder metal ion coordination by limiting the necessary conformational adjustments for optimal Zn 2+ binding. These insights into the structural changes underlying the function of short peptides offer valuable knowledge for the design of metal-dependent peptide-based catalysts.
Type of Medium:
Online Resource
ISSN:
2058-9689
Language:
English
Publisher:
Royal Society of Chemistry (RSC)
Publication Date:
2023
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