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Article

Hydrogen Bonding and Solvation of a Proline-Based Peptide Model in Salt Solutions

1
European Laboratory for Non-Linear Spectroscopy, LENS, Via Nello Carrara, 1, 50019 Sesto Fiorentino, Italy
2
Elettra-Sincrotrone Trieste, S.S. 114 km 163.5, Basovizza, 34149 Trieste, Italy
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Area Science Park, Padriciano, 99, 34149 Trieste, Italy
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Dipartimento di Chimica, Biologia e Biotecnologie, Università di Perugia, Via Elce di Sotto, 8, 06123 Perugia, Italy
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Dipartimento di Scienze, Università degli Studi Roma Tre, Via della Vasca Navale, 84, 00146 Roma, Italy
*
Author to whom correspondence should be addressed.
Academic Editor: Maria Grazia Ortore
Life 2021, 11(8), 824; https://doi.org/10.3390/life11080824
Received: 26 July 2021 / Revised: 7 August 2021 / Accepted: 9 August 2021 / Published: 12 August 2021
The hydrogen bonding of water and water/salt mixtures around the proline-based tripeptide model glycyl-l-prolyl-glycinamide·HCl (GPG-NH2) is investigated here by multi-wavelength UV resonance Raman spectroscopy (UVRR) to clarify the role of ion–peptide interactions in affecting the conformational stability of this peptide. The unique sensitivity and selectivity of the UVRR technique allow us to efficiently probe the hydrogen bond interaction between water molecules and proline residues in different solvation conditions, along with its influence on trans to cis isomerism in the hydrated tripeptide. The spectroscopic data suggest a relevant role played by the cations in altering the solvation shell at the carbonyl site of proline., while the fluoride and chloride anions were found to promote the establishment of the strongest interactions on the C=O site of proline. This latter effect is reflected in the greater stabilization of the trans conformers of the tripeptide in the presence of these specific ions. The molecular view provided by UVRR experiments was complemented by the results of circular dichroism (CD) measurements that show a strong structural stabilizing effect on the β-turn motif of GPG-NH2 observed in the presence of KF as a co-solute. View Full-Text
Keywords: peptide; hydrogen bonding; proline; UV resonance Raman peptide; hydrogen bonding; proline; UV resonance Raman
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MDPI and ACS Style

Catalini, S.; Rossi, B.; Tortora, M.; Foggi, P.; Gessini, A.; Masciovecchio, C.; Bruni, F. Hydrogen Bonding and Solvation of a Proline-Based Peptide Model in Salt Solutions. Life 2021, 11, 824. https://doi.org/10.3390/life11080824

AMA Style

Catalini S, Rossi B, Tortora M, Foggi P, Gessini A, Masciovecchio C, Bruni F. Hydrogen Bonding and Solvation of a Proline-Based Peptide Model in Salt Solutions. Life. 2021; 11(8):824. https://doi.org/10.3390/life11080824

Chicago/Turabian Style

Catalini, Sara, Barbara Rossi, Mariagrazia Tortora, Paolo Foggi, Alessandro Gessini, Claudio Masciovecchio, and Fabio Bruni. 2021. "Hydrogen Bonding and Solvation of a Proline-Based Peptide Model in Salt Solutions" Life 11, no. 8: 824. https://doi.org/10.3390/life11080824

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