Journal ArticleDOI
Can Helical Peptides Unwind One Turn at a Time? ‐ Controlled Conformational Transitions in α,β2,3‐Hybrid Peptides
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TLDR
Unfolding of helical trans-β(2,3) -hybrid peptides with (α-β)n α composition proceeded in a systematic manner with the turns unwinding sequentially; C-terminal region of these peptides were first to unwind and the process propagated towards N terminus.Abstract:
Unfolding of helical trans-β(2,3) -hybrid peptides with (α-β)n α composition, when executed by increasing solvent polarity or temperature, proceeded in a systematic manner with the turns unwinding sequentially; C-terminal region of these peptides were first to unwind and the process propagated towards N terminus with more and more β residues equilibrating from the gauche to the anti rotameric state across Cα-Cβ . This is evidenced by clear change in their Cβ H signal splitting, (3)JCαH-CβH values, and sequential disappearance of i,i+2 NOEs.read more
Citations
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Towards a fragment-based approach in gelator design: halogen effects leading to thixotropic, mouldable and self-healing systems in aryl-triazolyl amino acid-based gelators!
TL;DR: A simple replacement of a H atom by Br transformed non-gelating aryl triazolyl amino acid benzyl ester into a versatile gelator, which formed shape-persistent, self-healing and mouldable gels.
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Aryl-triazolyl peptides for efficient phase selective gelation and easy removal of dyes from water
TL;DR: Fine-tuning the gelation ability of aryl triazolyl peptide 1 by C-terminal modification led to the identification of 2 with the remarkable ability to form highly transparent gels in a wide range of solvents including oils.
Journal ArticleDOI
Sulfamide-Lattice Restructuring To Form Dimensionally Controlled Molecular Arrays and Gel-Forming Systems
Saripalli V. Raghava,Pushparathinam Gopinath,Bhartendu K. Srivastava,Venkatachalam Ramkumar,K. M. Muraleedharan +4 more
TL;DR: Crystallographic studies of these two-component systems gave molecular-level insight into the assembly and showed the importance of anisotropy in the distribution of secondary interactions in gelation.
Journal ArticleDOI
Determining Factors for the Unfolding Pathway of Peptides, Peptoids, and Peptidic Foldamers.
TL;DR: Using force-probe molecular dynamics, this work identifies the determining structural factors for the unfolding pathways and reveals the interplay between the hydrogen bond strength and the backbone rigidity in the stabilization of their helix conformations.
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Modulating the Structural Properties of α,γ-Hybrid Peptides by α-Amino Acid Residues: Uniform 12-Helix Versus “Mixed” 12/10-Helix
TL;DR: The results presented here emphasize the influence of the structure of the α-amino acid residues in dictating the helix types in α,γ-hybrid peptide foldamers and demonstrate the consequences for folding of small structural variations in the monomers.
References
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Structural characteristics of .alpha.-helical peptide molecules containing Aib residues
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The world of beta- and gamma-peptides comprised of homologated proteinogenic amino acids and other components.
TL;DR: Tests with proteolytic enzymes of all types and in vivo examination showed β‐ and γ‐peptides to be completely stable towards proteolysis and, as demonstrated for two β‐ peptides, extraordinarily stable towards metabolism, even when bearing functionalized side chains.
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Foldamers with Heterogeneous Backbones
W. Seth Horne,Samuel H. Gellman +1 more
TL;DR: The promise of heterogeneous backbone foldamers is illustrated by focusing on examples containing both alpha- and beta-amino acid residues, which offer new platforms for mimicry of the molecular surfaces involved in specific protein-protein recognition events.
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Design of folded peptides.
TL;DR: Examination of protein 3-dimensional structures suggests that complex tertiary folds and quaternary associations can be deconstructed into a limited number of secondary structural elements, such as strands, helices, and turns, which are assembled using loosely structured loops.