2023
DOI: 10.1039/d3sm00339f
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Effect of the spacer on the structure and self-assembly of FF peptide mimetics

Abstract: We have designed and synthesized a series of FF peptide mimetic with conformationally rigid and flexible spacers to study the effect of spacers on their structure and self-assembly. The results...

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Cited by 5 publications
(3 citation statements)
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“…Moreover, the amino acid bound to surfaces can promote hydroxyapatite crystallization by attracting Ca 2+ and PO 4 3− ions [26] . Phenylalaine derivatives are well studied gelator [20,27,28] . Considering the reversibility, trigger ability, tenable mechanical and thermal stability of the generated gels, we have used the gel to imitate the extracellular matrix and encourage the formation and encapsulation of hydroxyapatite (ESI Table S2).…”
Section: Resultsmentioning
confidence: 99%
See 1 more Smart Citation
“…Moreover, the amino acid bound to surfaces can promote hydroxyapatite crystallization by attracting Ca 2+ and PO 4 3− ions [26] . Phenylalaine derivatives are well studied gelator [20,27,28] . Considering the reversibility, trigger ability, tenable mechanical and thermal stability of the generated gels, we have used the gel to imitate the extracellular matrix and encourage the formation and encapsulation of hydroxyapatite (ESI Table S2).…”
Section: Resultsmentioning
confidence: 99%
“…[26] Phenylalaine derivatives are well studied gelator. [20,27,28] Considering the reversibility, trigger ability, tenable mechanical and thermal stability of the generated gels, we have used the gel to imitate the extracellular matrix and encourage the formation and encapsulation of hydroxyapatite (ESI Table S2). The FE-SEM images (Figure 7) show that the orientation and integration of apatite nanocrystals match those of biologically mineralized collagen fibrils, the fundamental constituents of bone.…”
Section: Resultsmentioning
confidence: 99%
“…13–16 Peptide assemblies are ordinarily governed by a combination of noncovalent and covalent interactions, encompassing hydrogen bonds, 17 π–π stacking, 18 hydrophobic interactions, 19,20 coulombic forces, 21,22 disulfide S–S bonds, 23,24 l -phenylalanine polymerization, dityrosine crosslinking, 25–27 and so on, which could drive peptide self-assembly processes, stabilize secondary or tertiary structures, and establish conjugation patterns even at the protein level. Tremendous efforts have been made to exploit de novo designed peptides and mimic bioactive assemblies, however, the function-oriented synthesis is still limited by many influencing factors of pH environment, 28–30 working temperature, 31–33 ionic strength, 34,35 hydrophilic/hydrophobic properties, 36,37 pre-assembly method, 38,39 host–guest modeling, 40,41 spacer occupation, 42,43 and so on.…”
Section: Introductionmentioning
confidence: 99%