Hydrophobic nanofibers: a peptide-based functional anti-fouling material

Hati, Kshitish Chandra; Kumar, Santosh; Mondal, Sahabaj; Nandi, Sujay Kumar; Singh, Surajit; Shit, Ananda; Haldar, Debasish

doi:10.1039/d2ma00084a

Cited by 1 publication

(3 citation statements)

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“…It forms supramolecular right-handed helical assemblies with small internal pores (Figure , top). The development of β-peptides, cyclic peptides, peptoids, and synthetic foldamers able to form helices or tubular structures has attracted great attention in the last few decades. − However, the fabrication of supramolecular helical assemblies from short α-peptides with a defined secondary structure is relatively rare. − In this case, it is composed by four dimers stabilized by H-bonds between the CO (Alloc) and CO i +1 of molecule A and the NH i +1 and NH i +2 of molecule B, respectively (Figure , bottom). In addition, the structure is stabilized by a set of interdimer H-bonds.…”

Section: Resultsmentioning

confidence: 99%

“… 68 − 71 However, the fabrication of supramolecular helical assemblies from short α-peptides with a defined secondary structure is relatively rare. 17 − 20 In this case, it is composed by four dimers stabilized by H-bonds between the CO (Alloc) and CO i +1 of molecule A and the NH i +1 and NH i +2 of molecule B, respectively ( Figure 4 , bottom). In addition, the structure is stabilized by a set of interdimer H-bonds.…”

Section: Resultsmentioning

confidence: 99%

“…Interestingly, the β-turn structure was found to be crucial for other applications apart from medicinal chemistry, such as peptide-based catalysis and self-assembly. Figure b shows an example of a β-turn-containing short peptide able to catalyze the atroposelective bromination of pharmaceutically relevant quinazolinones with high levels of enantioinduction. , In addition, β-turns have been exploited in the search of novel peptide-based materials. − As an example, a tetrapeptide model containing Leu, Aib (α-aminoisobutyric acid), and Ser adopts a type-III′ β-turn, which self-assembles to form a supramolecular nanotube in the solid state (Figure c) …”

Section: Introductionmentioning

confidence: 99%

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β-Turn Induction by a Diastereopure Azepane-Derived Quaternary Amino Acid

Núñez-Villanueva,

Plata-Ruiz,

Romero-Muñiz

et al. 2023

J. Org. Chem.

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β-Turns are one of the most common secondary structures found in proteins. In the interest of developing novel βturn inducers, a diastereopure azepane-derived quaternary amino acid has been incorporated into a library of simplified tetrapeptide models in order to assess the effect of the azepane position and peptide sequence on the stabilization of β-turns. The conformational analysis of these peptides by molecular modeling, NMR spectroscopy, and X-ray crystallography showed that this azepane amino acid is an effective β-turn inducer when incorporated at the i + 1 position. Moreover, the analysis of the supramolecular selfassembly of one of the β-turn-containing peptide models in the solid state reveals that it forms a supramolecular helical arrangement while maintaining the β-turn structure. The results here presented provide the basis for the use of this azepane quaternary amino acid as a strong β-turn inducer in the search for novel peptide-based bioactive molecules, catalysts, and biomaterials.

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