Molecular complementarity and structural heterogeneity within co-assembled peptide β-sheet nanofibers

Abstract

Charge-complementary peptides organize into co-assembled β-sheet nanofibers composed of multiple substructures rather than a single structure as seen in self-assembling peptides.

Injectable nanofibrillar hydrogels based on charge-complementary peptide co-assemblies

“…Replacing neutral residues with charged residues in known synthetic self-assembling peptide sequences is an effective way to encode selective co-assembly because like-charged molecules repel each other, while opposites attract. 12,32,33 For example, the pair referred to as Co-Assembly Tags based on Charge complementarity, or "CATCH(+/−)" are 11 amino acid long variants of the selfassembling peptide Q11, 12,34,35 P11-13 and P11-14 were derived from P11-2, 32 and KVW10 and EVW10 are variants of MAX1. 36 Selective co-assembly of charge-complementary peptides can be triggered at physiologic temperature, pH, and ionic strength, which makes these systems ideal for encapsulating cells or creating hydrogels with immobilized protein domains.…”

Nanostructure, Self-Assembly, Mechanical Properties, and Antioxidant Activity of a Lupin-Derived Peptide Hydrogel

“…Since the β-sheet structure is characteristic of amyloid-like fibers, which are well established to be one of the basic functional motifs of self-assembling peptide molecules [32], we examined this behavior on BT13 peptide using the thioflavin-T (ThT) binding assay, an amyloid-specific fluorescent dye [33,34]. Staining the BT13 peptide sample with ThT resulted in high fluorescence levels compared to T13 peptide (Figure 1c), with a typical amyloid-binding emission signal (centered at 490 nm), establishing its β-sheet-rich amyloidlike nature, similar to other self-assembling peptides found in the literature [35][36][37][38][39][40].…”

“…Biomedicines 2021, 9, x FOR PEER REVIEW 5 of 12 [32], we examined this behavior on BT13 peptide using the thioflavin-T (ThT) binding assay, an amyloid-specific fluorescent dye [33,34]. Staining the BT13 peptide sample with ThT resulted in high fluorescence levels compared to T13 peptide (Figure 1c), with a typical amyloid-binding emission signal (centered at 490 nm), establishing its β-sheet-rich amyloid-like nature, similar to other self-assembling peptides found in the literature [35][36][37][38][39][40]. Finally, we sought to investigate the nanostructures of T13 and BT13 peptides by AFM, which allows for examination of the fiber distribution of the assemblies (Figure 2a,b).…”

Heteronuclear and homonuclear radio-frequency-driven recoupling

“…Since then, the homonuclear radio-frequencydriven recoupling (RFDR) sequence (Bennett et al, 1992) has been successfully applied for the qualitative and quantitative determinations of the dipolar spin correlations in materials (Saalwächter, 2013;Messinger et al, 2015;Fritz et al, 2019;Roos et al, 2018;Nishiyama et al, 2014a;Wong et al, 2020;Hellwagner et al, 2018;Pandey and Nishiyama, 2018) and biomolecular samples (Zheng et al, 2007;Tang et al, 2011;Shen et al, 2012;Pandey et al, 2014;Grohe et al, 2019;Andreas et al, 2015;Petkova et al, 2002;Aucoin et al, 2009;Zinke et al, 2018;Zhang et al, 2017;Zhou et al, 2012;Jain et al, 2017;Colvin et al, 2015;Shi et al, 2015;Daskalov et al, 2021). Sun et al (1995) showed that the RFDR pulse sequence element could also be used as a part of the SPICP experiment (Wu and Zilm, 1993) for removing the undesired effect of the chemical shift terms to zero order.…”