Self-assembling tripeptide forming water-bound channels and hydrogels

被引：9
作者：
Parisi, Evelina [1 ]
Adorinni, Simone [1 ]
Garcia, Ana M. [1 ]
Kralj, Slavko [2 ,3 ]
De Zorzi, Rita [1 ]
Marchesan, Silvia [1 ,4 ]
机构：
[1] Univ Trieste, Dept Chem & Pharmaceut Sci, Trieste, Italy
[2] Jozef Stefan Inst, Dept Mat Synth, Ljubljana, Slovenia
[3] Univ Ljubljana, Fac Pharm, Dept Pharmaceut Technol, Ljubljana, Slovenia
[4] Univ Trieste, Dept Chem & Pharmaceut Sci, I-34127 Trieste, Italy
来源：
JOURNAL OF PEPTIDE SCIENCE | 2023年 / 29卷 / 11期
关键词：
gels; hydrogels; nanofibril; self-assembly; CIRCULAR-DICHROISM; TRYPTOPHAN FLUORESCENCE; AMINO-ACIDS; DESIGN; FABRICATION; MECHANISM; PEPTIDES; FMOC;
D O I：
10.1002/psc.3524
中图分类号：
Q5 [生物化学]; Q7 [分子生物学];
学科分类号：
071010 ; 081704 ;
摘要：
D-Ser(tBu)-L-Phe-L-Trp is described as a self-assembling tripeptide that yields nanofibrillar hydrogels at physiological conditions (phosphate buffer at pH 7.4). The peptide is characterized by several spectroscopic methods, such as circular dichroism and fluorescence, oscillatory rheometry, and transmission electron microscopy. Single-crystal X-ray diffraction reveals supramolecular packing into water-bound channels and allows the visualization of the intermolecular interactions holding together peptide stacks.
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页数：6
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