Phase-transition of hydrophobic dipeptide L-phenylalanyl-L-alanine under high pressure via Raman spectroscopy

被引:1
作者
Cordeiro, Adrya J. P. [1 ]
Alves, Kelly C. [2 ]
Mota, Elder A. V. [3 ]
Vasconcelos, Daniel L. M. [4 ]
Lima, Raphaela A. [1 ]
da Silva, Jose A. S. [1 ]
Freire, Paulo T. C. [1 ]
机构
[1] Univ Fed Ceara, Dept Phys, BR-60021970 Fortaleza, CE, Brazil
[2] Fed Univ Para, Technol Inst, BR-66075110 Belem, PA, Brazil
[3] Fed Univ Para, Fac Sci & Technol, BR-68440000 Abaetetuba, PA, Brazil
[4] Univ Estadual Ceara, Fac Educ Sci & Letter Cent Hinterland, BR-63902098 Quixada, CE, Brazil
关键词
Raman Spectroscopy; Hydrophobic dipeptide; L-Phenylalanyl-L-Alanine; High pressure;
D O I
10.1016/j.saa.2024.125290
中图分类号
O433 [光谱学];
学科分类号
0703 ; 070302 ;
摘要
The study conducted on L-Phenylalanyl-L-Alanine (C12H16N2O3) dehydrated crystals under high-pressure conditions up to 7.0 GPa using Raman spectroscopy revealed significant modifications in both lattice and internal modes. Particularly, alterations were observed in modes associated with carbonyl and NH2 functionalities around 1600 cm(-1). The Raman spectra exhibited distinct changes in modes related to torsions and stretching of the ring, suggesting a potential conformational change in specific pressure intervals: 2.6-3.0 GPa, and 5.0-5.1 GPa. Furthermore, notable changes between 0.4 and 1.0 GPa hinted at a structural transformation in the crystal. Additionally, Scanning Electron Microscopy-Field Emission Gun (SEM-FEG) was employed to elucidate the crystal pattern of Phe-Ala center dot 2H(2)O. The ambient study, incorporating calculations, infrared, and Raman spectroscopy, contributed to a comprehensive understanding of vibrational mode assignments. This research sheds light on the behavior of L-Phenylalanyl-L-Alanine dehydrated crystals under varying pressure conditions, offering valuable insights for medicinal and pharmacological applications.
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页数:13
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