In this study we consider the features of spatial-structure formation in proteins and their application in bioengineering. Methods for the quantitative assessment of the chirality of regular helical and irregular structures of proteins are presented. The features of self-assembly of phenylalanine (F) into peptide nanotubes (PNT), which form helices of different chirality, are also analyzed. A method is proposed for calculating the magnitude and sign of the chirality of helix-like peptide nanotubes using a sequence of vectors for the dipole moments of individual peptides.
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http://dx.doi.org/10.3390/nano11123299 | DOI Listing |
ACS Appl Mater Interfaces
January 2025
Air Force Research Laboratory, 711th Human Performance Wing, Wright-Patterson Air Force Base, Wright-Patterson AFB, Ohio 45433, United States.
Peptides, due to their diverse and controllable properties, are used as both liquid and gas phase recognition elements for both biological and chemical targets. While it is well understood how binding of a peptide to a biomolecule can be converted into a sensing event, there is not the same mechanistic level of understanding with regard to how peptides modulate the selectivity of semiconductor/conductor-based gas sensors. Notably, a rational, mechanistic study has not yet been performed to correlate peptide properties to the sensor response for volatile organic compounds (VOCs) as a function of chemical properties.
View Article and Find Full Text PDFChem Sci
December 2024
Department of Chemistry, University of Warwick Coventry CV4 7AL UK
Self-assembling cyclic peptide nanotubes are fascinating supramolecular systems with promising potential for various applications, such as drug delivery, transmembrane ionic channels, and artificial light-harvesting systems. In this study, we present novel pH-responsive nanotubes based on asymmetric cyclic peptide-polymer conjugates. The pH response is introduced by a tertiary amine-based polymer, poly(dimethylamino ethyl methacrylate) (pDMAEMA) or poly(diethylamino ethyl methacrylate) (pDEAEMA) which is protonated at low pH.
View Article and Find Full Text PDFAngew Chem Int Ed Engl
December 2024
South China Advanced Institute for Soft Matter Science and Technology, School of Emergent Soft Matter, South China University of Technology, Guangzhou, 510640, China.
Cross-β structures are crucial in driving protein folding and aggregation. However, due to their strong aggregating tendency, the precise control of the self-assembly of β-sheet-forming peptides remains a challenge. We propose a molecular geometry strategy to study and control the self-assembly of cross-β structures.
View Article and Find Full Text PDFInt J Biol Macromol
December 2024
Department of Emergency Medicine, The First Affiliated Hospital of Zhengzhou University, Zhengzhou 450052, China. Electronic address:
Antibiotic abuse has led to an increasingly serious risk of antimicrobial resistance, developing alternative antimicrobials to combat this alarming issue is urgently needed. Rhesus theta defensin-1 (RTD-1) is a theta-defensin contributing to broad-spectrum bactericidal activity via the mechanisms of membrane perturbation. Intriguingly, human defensin-6 (HD6), an enteric defensin secreted by Paneth cells without direct bactericidal effect, could self-assembled into fibrous networks to trap enteric pathogens for assistance of innate immunity.
View Article and Find Full Text PDFLangmuir
December 2024
Department of Chemistry, Laboratory of Peptide and Amyloid Research, Indian Institute of Technology Guwahati, Guwahati 781039, Assam, India.
Peptides possess a remarkable propensity to adopt distinct morphologies, ranging from simple aggregates to complex structures such as fibrils and nanotubes. Morphology transformation in peptides is intricately linked to the physicochemical properties of peptides and external factors such as pH, temperature, and solvent conditions. Thus, it is more complex.
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