Crystal structure of a tripeptide containing aminocyclododecane carboxylic acid: a supramolecular twisted parallel β-sheet in crystals

Vasudev, Prema G.; Aravinda, Subrayashastri; Shamala, Narayanaswamy

doi:10.1002/psc.2854

Cited by 3 publications

(2 citation statements)

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“…It formed a unique twisted parallel betasheet structure, which folds into a helical conformation in higherorder. [31] Moreover, SC-XRD data revealed that hetero chiral F-DNva-F creates a water channel, and homochiral FAF constructs layer structure in crystal packing. [36] In our experiments, SC-XRD data suggested that five of the stereoisomers built a parallel betasheet arrangement through several hydrogen bonding and hydrophobic interactions.…”

Section: Resultsmentioning

confidence: 99%

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Crystal structure and supramolecular arrangement of heterochiral tripeptides

et al. 2021

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The self-assembly properties of all possible stereoisomers of terminally protected Boc-Val-Phe-Phe-OMe, having sequence homogeneity with Alzheimer's amyloidbeta (Aβ 18-20 ) peptide was investigated. The morphology analysis by field emission scanning microscope (FE-SEM) revealed that protected VFF and vff (small letters denote one letter code of D-amino acids) exhibited a ribbon-like fibrous network, vFF, Vff, VfF, and vFf formed rod-like structures. Although VFf exhibited a mixture of two morphologies (rod-like and spherical), vfF showed spherical structures predominantly. The single-crystal X-ray diffraction (SC-XRD) indicated that five of the stereoisomers formed a parallel beta-sheet arrangement. In higher-order packing, while Vff, VfF, and vFf exhibited supramolecular sheet-like architecture, VFf and vfF pair showed helical sheet-like arrangement. All corresponding enantiomers displayed identical morphology but opposite conformation. The chirality of amino acids in peptides played a significant role in their supramolecular arrangements. Interestingly, all self-aggregated peptides can bind with amyloid binding dye thioflavin T.

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Section: Resultsmentioning

confidence: 99%

“…[28][29][30] Shamala et al reported the crystal structure of tripeptide Boc-Leu-Val-Ac 12 c-OMe (Ac 12 c = 1-aminocyclododecane-1-carboxylic acid), which formed a twisted beta-sheet structure. [31] On the other hand, the gelation behavior of the central hydrophobic region of the Aβ peptide was also investigated. Haldar et al…”

Section: Introductionmentioning

confidence: 99%

Crystal structure and supramolecular arrangement of heterochiral tripeptides

et al. 2021

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Self-Assembly and Wound Healing Activity of Biomimetic Cycloalkane-Based Lipopeptides

Adak,

Castelletto,

Hamley

et al. 2024

ACS Appl. Mater. Interfaces

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The self-assembly of lipopeptide (peptide amphiphile) molecules bearing single linear lipid chains has been widely studied, as has their diverse range of bioactivities. Here, we introduce lipopeptides bearing one or two cycloalkane chains (cycloheptadecyl or cyclododecyl) conjugated to the collagen-stimulating pentapeptide KTTKS used in Matrixyl formulations. The self-assembly of all four molecules is probed using fluorescence probe measurements to detect the critical aggregation concentration (CAC), and cryogenic-TEM and small-angle X-ray scattering (SAXS) to image the nanostructure. The peptide conformation is studied using circular dichroism (CD) and FTIR spectroscopies. All the cycloalkane lipopeptides show excellent compatibility with dermal fibroblasts. The compounds bearing one or two cyclododecyl chains (denoted as DKT and DDKT, respectively) show wound healing in diabetic rats, the improvement being markedly enhanced for DDKT. Interestingly, the revival of hair follicles and blood vessels in the dermis were observed, which are the critical markers of effective wound repair. Analysis of H&E-stained tissue images (from a rat model) shows that the rat groups treated with DDKT and DKT displayed a significantly increased amount of regenerated hair follicles, indicating a faster healing process for DDKT compared to the control group. Collagen deposition was also enhanced, especially for DDKT, and by day 20, the DDKT-treated groups had developed a dense collagen network accompanied by a regenerated epidermis. At the same time, the number of blood vessels in DDKT-treated diabetic wounds was significantly higher than in control groups and neovascularization was substantially enhanced, as assayed using α-SMA (a marker for vascular smooth muscle cells) and CD31 (a marker specific to vascular endothelial cells). These results suggest that the lead lipopeptide DDKT exhibits a remarkable pro-vascularization capability and shows great promise for future application as a wound-healing biomaterial.

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Sequence-Dependent Nanofiber Structures of Phenylalanine and Isoleucine Tripeptides

Xiong¹,

Liu²,

Han³

2020

IJMS

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The molecular design of short peptides to achieve a tailor-made functional architecture has attracted attention during the past decade but remains challenging as a result of insufficient understanding of the relationship between peptide sequence and assembled supramolecular structures. We report a hybrid-resolution model to computationally explore the sequence–structure relationship of self-assembly for tripeptides containing only phenylalanine and isoleucine. We found that all these tripeptides have a tendency to assemble into nanofibers composed of laterally associated filaments. Molecular arrangements within the assemblies are diverse and vary depending on the sequences. This structural diversity originates from (1) distinct conformations of peptide building blocks that lead to different surface geometries of the filaments and (2) unique sidechain arrangements at the filament interfaces for each sequence. Many conformations are available for tripeptides in solution, but only an extended β-strand and another resembling a right-handed turn are observed in assemblies. It was found that the sequence dependence of these conformations and the packing of resulting filaments are determined by multiple competing noncovalent forces, with hydrophobic interactions involving Phe being particularly important. The sequence pattern for each type of assembly conformation and packing has been identified. These results highlight the importance of the interplay between conformation, molecular packing, and sequences for determining detailed nanostructures of peptides and provide a detailed insight to support a more precise design of peptide-based nanomaterials.

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Crystal structure of a tripeptide containing aminocyclododecane carboxylic acid: a supramolecular twisted parallel β-sheet in crystals

Cited by 3 publications

References 73 publications

Crystal structure and supramolecular arrangement of heterochiral tripeptides

Crystal structure and supramolecular arrangement of heterochiral tripeptides

Self-Assembly and Wound Healing Activity of Biomimetic Cycloalkane-Based Lipopeptides

Sequence-Dependent Nanofiber Structures of Phenylalanine and Isoleucine Tripeptides

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