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Conformational Studies of Proteins and Peptides

A special issue of International Journal of Molecular Sciences (ISSN 1422-0067). This special issue belongs to the section "Molecular Biophysics".

Deadline for manuscript submissions: 10 July 2024 | Viewed by 1326

Special Issue Editors


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Guest Editor
Instituto de Estructura de la Materia, IEM-CSIC, Serrano 121, 28006 Madrid, Spain
Interests: molecular biophysics; optical spectroscopy; biomolecular structure and dynamics

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Guest Editor
Instituto de Estructura de la Materia, IEM-CSIC, Serrano 121, 28006 Madrid, Spain
Interests: plasmonic nanoparticles; surface enhanced Raman scattering; optical spectroscopy
Special Issues, Collections and Topics in MDPI journals

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Guest Editor
LVTS, INSERM U1148, Université Sorbonne Paris Nord, 74 rue Marcel Cachin, 93017 Bobigny Cédex, France
Interests: biophysics; peptide structure; protein structure; optical spectroscopies; Raman scattering; FT-IR absorption

Special Issue Information

Dear Colleagues,

Proteins and linear heteropolymers, the backbone of which is formed by successive peptide bonds between natural amino acids, provide a wealth of structural properties. Despite the fact that the conformational flexibility of each polymer residue is simply governed by three torsion angles (f, y, w), a variety of forms is expected in relation to the values assigned to these angles (helices, sheets, and turns, etc.). With structure and function being closely related in proteins, the global conformation adopted by a peptide chain determines its function. The surrounding water molecules and their dynamics also play a pivotal role in the chain folding of globular proteins, in maintaining the disordered character of chains, and in inducing their aggregation processes, which are known as the main cause of several human diseases such as Alzheimer’s, Parkinson’s and type‑II diabetes. Short size peptide chains are recognized as efficient bioactive, functional and imaging agents. Their versatility for elaborating therapeutic agents, used, for instance, as analogues of natural hormones, as well for as innovating synthetic materials has been emphasized over the past two decades. In this Special Issue, our aim is to explore the capability of different physical techniques such as X-ray diffraction/scattering, NMR, optical spectroscopies (electronic circular dichroism, FT-IR absorption, vibrational circular dichroism, Raman scattering, Raman optical activity), in combination with adequate theoretical methods, to elucidate the structural features of proteins and peptides.

Prof. Dr. Mahmoud Ghomi
Dr. Santiago Sanchez-Cortés
Dr. Belén Hernández
Guest Editors

Manuscript Submission Information

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Published Papers (1 paper)

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Research

12 pages, 1366 KiB  
Article
Steady-State and Time-Resolved Fluorescence Study of Selected Tryptophan-Containing Peptides in an AOT Reverse Micelle Environment
by Krystian Gałęcki, Agnieszka Kowalska-Baron, Katarzyna E. Nowak, Anna Gajda and Beata Kolesińska
Int. J. Mol. Sci. 2023, 24(20), 15438; https://doi.org/10.3390/ijms242015438 - 22 Oct 2023
Viewed by 1042
Abstract
The aim of this study was to demonstrate the utility of time-resolved fluorescence spectroscopy in the detection of subtle changes in the local microenvironment of a tryptophan chromophore in a confined and crowded medium of AOT reverse micelles, which mimic biological membranes and [...] Read more.
The aim of this study was to demonstrate the utility of time-resolved fluorescence spectroscopy in the detection of subtle changes in the local microenvironment of a tryptophan chromophore in a confined and crowded medium of AOT reverse micelles, which mimic biological membranes and cell compartmentalization. For this purpose, fluorescence properties of L-tryptophan and several newly synthesized tryptophan-containing peptides in buffer and in an AOT reverse micelle medium were determined. It was shown that insertion of tryptophan and its short di- and tripeptides inside micelles led to evident changes in both the steady-state emission spectra and in fluorescence decay kinetics. The observed differences in spectral characteristics, such as a blue shift in the emission maxima, changes in the average fluorescence lifetime, and the appearance of environmental-dependent fluorescent species, showed the utility of time-resolved fluorescence spectroscopy as a sensitive tool for detecting subtle conformational modifications in tryptophan and its peptides induced by changes in polarity, viscosity, and specific interactions between chromophores and water molecules/polar groups/ions that occur inside reverse micelles. Full article
(This article belongs to the Special Issue Conformational Studies of Proteins and Peptides)
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