Structural consequences ofD-amino acids in collagen triple-helical peptides

Shah, Nikhil R.; Brodsky, Barbara; Kirkpatrick, Alan; Ramshaw, John A. M.

doi:10.1002/(sici)1097-0282(19990405)49:4<297::aid-bip4>3.0.co;2-q

Cited by 30 publications

(6 citation statements)

References 25 publications

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“…For the assemblies of the variants, the measured angles are about 33° and are not noticeably affected by chiral switching of the amino acids. The results reveal that switching chirality of just one residue of peptides can destabilize its assembly on the surface, which is in close agreement with the data obtained in solution, indicating d -amino acid substitution results in destruction of β-sheet conformation. , It was reported that the d -amino acid broke secondary structures of peptides − ,, and could stabilize the turn structure. ,, This kind of effect on the main chain of the peptides could contribute to the destabilization of peptide assembly on surface. In addition, the change of side chain orientation perhaps perturbs the original assembly structure, for the previous results showed the instinctive property and modification of side chain exerted significant influence on peptide assembly. , Figure c shows the assembly model of the mutants, almost the same as that of Poly7Q.…”

supporting

confidence: 86%

“…The peptide-based structures are highly sequence-dependent and sensitive to amino acid composition in general, leading to a wide range of interactions that enable diversified functionalities. Interactions relating to amino acid chirality, such as stereochemical effects, have been predicted by Pauling and Corey in their pioneering studies in 1953, in which equimolar mixtures of a parent peptide and its enantiomer were observed to pack into rippled β-sheet structures that contain l - and d -sequences, and revisited recently by a number of investigations. − The intrinsic chirality of peptide could control the nanostructure of its self-assembled nanofibrils …”

mentioning

confidence: 99%

“…d -Amino acid replacement has been reported to disturb the original secondary structure of peptides. For example, chiral conversion of amino acids destabilizes α-helix − and β-sheet , structure and the helix-destabilizing ability is highly dependent on the steric hindrance of amino acid side chains . In addition, it is suggested that replacing Gly residues with d -amino acids does not change the native structure of proteins. − In recent years, enantiomeric peptides have been shown to coassemble into fibrils that feature alternating l - and d -peptide, − contrary to the results that mixtures of enantiomeric amyloid peptides fail to coassemble but self-sort into enantiomerically pure fibrils. , Hydrogels formed from racemic fibrils possess enhanced mechanical rigidity compared with pure enantiomeric gels formed from either peptide alone, which is due to maximized inter-residue hydrophobic interactions between enantiomers. , As a result, chirality effects are extensively exploited to mediate structure, enhance proteolytic stability, and control bulk properties of peptide-based nanomaterials.…”

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confidence: 99%

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Steric Dependence of Chirality Effect in Surface-Mediated Peptide Assemblies Identified with Scanning Tunneling Microscopy

Zheng

Zou

et al. 2019

Nano Lett.

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Amino acid chirality has been recognized as an important driving force in constructing peptide architectures, via interactions such as chirality-induced stereochemical effect. The introduction of site-specific chiral conversion of l- and d-amino acids in peptide sequences could enable the pursuit of the chirality effects in peptide assembly. In this work, we characterized the assemblies of heptapeptides with various side chain moieties and their chiral variants using STM. Specifically, two pairs of amino acids, Gln (Q) and Asn (N), Glu (E) and Asp (D), having one methylene difference in their side chains, are selected to elucidate the steric dependence of amino acid chiral effects on surface-bound peptide assemblies. The observed heptapeptide assembly structures reveal that chirality switching of a single amino acid is able to destabilize the surface-mediated peptide assemblies, and this disturbance effect can be positively correlated with the steric hindrance of amino acid side chains. Furthermore, the strength of the impact due to chiral conversion on heptapeptide assembly structure is noticeably dependent on the mutation sites, indicative of structural heterogeneity of chiral effects. These results could contribute to the molecular insights of chirality-induced stereochemical interactions in peptide assembly.

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confidence: 99%

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confidence: 99%

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Steric Dependence of Chirality Effect in Surface-Mediated Peptide Assemblies Identified with Scanning Tunneling Microscopy

Zheng

Zou

et al. 2019

Nano Lett.

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“…12 Due to its rapid racemization, l -Asp to d -Asp isomerization has been more widely observed in biological systems and has been more widely studied. 13–15 It is well known that aspartic acid in a protein—whether from translation or from deamidation of asparagine—is prone to forming a stable succinimide ring intermediate following self-nucleophilic attack. Subsequent ring opening and/or stereo-inversion converts aspartate to one of four isomeric forms: l -Asp, d -Asp, l -isoAsp, and d -isoAsp.…”

Section: Introductionmentioning

confidence: 99%

Differentiating aspartic acid isomers and epimers with charge transfer dissociation mass spectrometry (CTD-MS)

Edwards

Julian

et al. 2022

Analyst

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“…Amino acid chirality has been recognized as an important design modality to construct peptide self-assembled nanomaterials with the desired structure and function. d -Amino acid incorporation into l -peptides can break their original secondary structures − and disrupt their assembly structures . Our previous results have revealed that altering the chirality of single amino acid residue could destabilize surface-mediated peptide assemblies, and the disturbance strength was dependent on the steric hindrance of amino acid side chains and the mutant sites .…”

Section: Introductionmentioning

confidence: 99%

Heterochirality-Mediated Cross-Strand Nested Hydrophobic Interaction Effects Manifested in Surface-Bound Peptide Assembly Structures

Zheng

Luo

et al. 2022

J. Phys. Chem. B

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Amino acid chirality has been envisioned as an important strategy to regulate structure and function of peptide self-assembled architectures. However, the molecular mechanism of chirality effects in peptide assemblies remains largely elusive. Here, the assembly structures of l-peptide polyphenylalanine F10 (FFFFFFFFFF) and block heterochiral peptide F5f5 (FFFFFfffff) composed of two FFFFF repeat blocks with opposite chirality were characterized at the single-molecule level by using scanning tunneling microscopy. Each peptide formed two distinctively different assembly structures on the HOPG surface, in which peptide chains took parallel and antiparallel β-sheet conformations, respectively. The molecular-level observations revealed that the staggered arrangement of cross-strand side chains achieved in the antiparallel β-sheet structure of the block heterochiral peptide facilitated intimate packing of side chains and maximized inter-residue van der Waals interactions, which led to more residues participating in assembly and greatly stabilized the β-sheet structure of the surface-bound peptide assembly, but such cross-strand nested interactions were not accessible in the heterochiral parallel β-sheet structure and the enantiomerically pure assembly structures. This work could contribute to the molecular insights of stereochemical interactions in peptide assemblies and feasibility of extending this block heterochirality pattern to other peptides with various lengths and amino acid compositions for structural regulations.

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Structural consequences ofD-amino acids in collagen triple-helical peptides

Cited by 30 publications

References 25 publications

Steric Dependence of Chirality Effect in Surface-Mediated Peptide Assemblies Identified with Scanning Tunneling Microscopy

Steric Dependence of Chirality Effect in Surface-Mediated Peptide Assemblies Identified with Scanning Tunneling Microscopy

Differentiating aspartic acid isomers and epimers with charge transfer dissociation mass spectrometry (CTD-MS)

Heterochirality-Mediated Cross-Strand Nested Hydrophobic Interaction Effects Manifested in Surface-Bound Peptide Assembly Structures

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