Boosting stability: a hierarchical approach for self-assembling peptide structures

被引：2

作者：

Balandin, Denys ^{[1
,2
]}

Szulc, Natalia ^{[3
]}

Bystranowska, Dominika ^{[4
]}

Gasior-Glogowska, Marlena ^{[5
]}

Kruszakin, Roksana ^{[6
]}

Szefczyk, Monika ^{[1
]}

机构：

[1] Wroclaw Univ Sci & Technol, Fac Chem, Dept Bioorgan Chem, Wybrzeze Wyspianskiego 27, PL-50370 Wroclaw, Poland

[2] Med Univ Graz, Otto Loewi Res Ctr, Dept Med Chem, Neue Stiftingtalstr 6, A-8010 Graz, Austria

[3] Wroclaw Univ Environm & Life Sci, Dept Phys & Biophys, Norwida 25, PL-50375 Wroclaw, Poland

[4] Wroclaw Univ Sci & Technol, Fac Chem, Dept Biochem Mol Biol & Biotechnol, Wybrzeze Wyspianskiego 27, PL-50370 Wroclaw, Poland

[5] Wroclaw Univ Sci & Technol, Fac Fundamental Problems Technol, Dept Biomed Engn, Wybrzeze Wyspianskiego 27, PL-50370 Wroclaw, Poland

[6] Polish Acad Sci, Hirszfeld Inst Immunol & Expt Therapy, Lab Instrumental Anal & Preparat, Rudolfa Weigla 12, PL-53114 Wroclaw, Poland

来源：

JOURNAL OF MATERIALS CHEMISTRY B | 2024年 / 12卷 / 41期

关键词：

INFRARED-SPECTROSCOPY; DESIGN;

D O I：

10.1039/d4tb01545b

中图分类号：

TB3 [工程材料学]; R318.08 [生物材料学];

学科分类号：

0805 ; 080501 ; 080502 ;

摘要：

The primary objective of this study was to implement a hierarchical approach to enhance the conformational stability of a selected group of peptides by incorporating trans-(1S,2S)-2-aminocyclopentanecarboxylic acid (trans-ACPC). The influence of residue mutation on the peptide structures was investigated using circular dichroism, analytical ultracentrifugation, and vibrational spectroscopy. The resulting nanostructures were examined via transmission electron microscopy. The incorporation of trans-ACPC led to increased conformational stability and self-assembling propensity in peptides containing constrained beta-amino acid residues. Our findings indicate that the nanostructure formation is influenced by all the positions within the coiled-coils.

引用

页码：10682 / 10691

页数：10

共 39 条

[11] Interplay among side chain sequence, backbone composition, and residue rigidification in polypeptide folding and assembly [J].