Self-Assembly of Left- and Right-Handed Molecular Screws

Xu, Fei; Khan, Imran; McGuinness, Kenneth N.; Parmar, Avanish Singh; Silva, Teresita; Murthy, N. Sanjeeva; Nanda, Vikas

doi:10.1021/ja4106545

Cited by 57 publications

(53 citation statements)

References 31 publications

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“…Moreover, other very recent, intriguing results will greatly stimulate additional research in the fundamental field (chiral helix···helix interactions) of biomolecular processes. They include (i) stereoselectivity of the self‐assembly of left‐handed and right‐handed peptide screws with generation of novel collagen triple helix mimetics, using (Pro‐Pro‐Gly) 10 enantiomeric sequences as minimal building blocks ; (ii) polymorphism complexity (twist, chirality, and handedness inversion) exhibited by self‐aggregated peptides resulting in amyloid fibrils ; and (iii) preferred handedness of helical foldamers induced upon interaction with a protein surface .…”

Section: Discussionmentioning

confidence: 99%

Handedness preference and switching of peptide helices. Part I: Helices based on protein amino acids

Crisma

Zotti

Formaggio³

et al. 2014

J. Pept. Sci.

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In this article, we review the relevant results obtained during almost 60 years of research on a specific aspect of stereochemistry, namely handedness preference and switches between right-handed and left-handed helical peptide structures generated by protein amino acids or appropriately designed, side-chain modified analogs. In particular, we present and discuss here experimental and theoretical data on three categories of those screw-sense issues: (i) right-handed/left-handed α-helix transitions underwent by peptides rich in Asp, specific Asp β-esters, and Asn; (ii) comparison of the preferred conformations adopted by helical host-guest peptide series, each characterized by an amino acid residue (e.g. Ile or its diastereomer aIle) endowed with two chiral centers in its chemical structure; and (iii) right-handed (type I)/left-handed (type II) poly-(Pro)n helix transitions monitored for peptides rich in Pro itself or its analogs with a pyrrolidine ring substitution, particularly at the biologically important position 4. The unique modular and chiral properties of peptides, combined with their relatively easy synthesis, the chance to shape them into the desired conformation, and the enormous chemical diversity of their coded and non-coded α-amino acid building blocks, offer a huge opportunity to structural chemists for applications to bioscience and nanoscience problems.

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Section: Discussionmentioning

confidence: 99%

Handedness preference and switching of peptide helices. Part I: Helices based on protein amino acids

Crisma

Zotti

Formaggio³

et al. 2014

J. Pept. Sci.

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“…mixing fibril-forming L-and D peptides leads to preferential formation of heterochiral β-sheet assemblies (19). The 30-mer peptide (L-Pro-L-Pro-Gly) 10 forms a collagen-like triple helix that is very soluble in aqueous solution, but Nanda and co-workers have found that mixing solutions of enantiomeric triple helices leads to a supramolecular assembly/precipitation process that apparently involves intimate interactions between enantiomeric trimers (20). None of these intriguing studies has provided atomic-resolution insight on heterochiral associations.…”

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confidence: 99%

High-resolution structures of a heterochiral coiled coil

Mortenson

Steinkruger

Kreitler

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

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Interactions between polypeptide chains containing amino acid residues with opposite absolute configurations have long been a source of interest and speculation, but there is very little structural information for such heterochiral associations. The need to address this lacuna has grown in recent years because of increasing interest in the use of peptides generated from D amino acids (D peptides) as specific ligands for natural proteins, e.g., to inhibit deleterious proteinprotein interactions. Coiled-coil interactions, between or among α-helices, represent the most common tertiary and quaternary packing motif in proteins. Heterochiral coiled-coil interactions were predicted over 50 years ago by Crick, and limited experimental data obtained in solution suggest that such interactions can indeed occur. To address the dearth of atomic-level structural characterization of heterochiral helix pairings, we report two independent crystal structures that elucidate coiled-coil packing between L-and D-peptide helices. Both structures resulted from racemic crystallization of a peptide corresponding to the transmembrane segment of the influenza M2 protein. Networks of canonical knobs-into-holes side-chain packing interactions are observed at each helical interface. However, the underlying patterns for these heterochiral coiled coils seem to deviate from the heptad sequence repeat that is characteristic of most homochiral analogs, with an apparent preference for a hendecad repeat pattern.D peptides | transmembrane peptides | racemic crystallization | racemic detergent | coiled coil P olypeptides comprising D-amino acid residues have been sources of growing interest for biological applications, often for functions that depend on recognition by specific natural proteins (1-3). D peptides offer identical versatility in terms of conformation and side-chain functionality relative to conventional peptides (composed of L-amino acid residues), but D peptides are impervious to the action of proteolytic enzymes, which should improve pharmacokinetic properties in vivo relative to those of conventional peptides. The engineering of D peptides to display defined protein-binding preferences is hindered, however, by the dearth of experimental information available for such complexes. Structural principles that are well-known to govern interactions between two L-polypeptide chains are not directly extensible to pairings between peptides of opposite chirality. Favorable heterochiral interactions (between L-and D peptides) that are analogous to homochiral associations between L peptides were postulated decades ago on the basis of geometrical considerations (4, 5). In a 1953 analysis of structural parameters governing coiled-coil formation between right-handed α-helices formed from L peptides, for example, Crick suggested that analogous assemblies should be accessible to pairs of right-and left-handed helices (4). In the same year, Pauling and Corey postulated that heterochiral peptide mixtures could form "rippled" β-sheet assemblies with backbo...

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“…For instance, bottom‐up assembly has been demonstrated for a number of collagen peptide triple helices . These higher order assemblies have relied on cysteine knots, aromatic and electrostatic interactions, stereochemistry and shape complementarity, and metal‐ligand complexation to promote assembly beyond the triple helix. In this way, a wide range of collagen peptide‐based materials have been generated, including fibrils, sheets, and three‐dimensional matrices.…”

Section: Introductionmentioning

confidence: 99%

Controlling the morphology of metal‐triggered collagen peptide assemblies through ligand alteration

Chmielewski

2015

Biopolymers

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A number of methods have been explored to promote the higher order assembly of collagen peptide triple helices. In one case, NCoH, a complex hierarchical metal-promoted assembly was observed to form micron-scaled florettes with a ruffled surface topology at the nanoscale. In an effort to elucidate the role of the ligands in this collagen peptide assemblage, we reduced the number of carboxylates within the N-terminal ligand to produce a new peptide, ICoH. A striking difference in the morphology of the metal-triggered material was observed with ICoH, with stacked arrays of nanofibrils predominating. As the peptide to metal ion ratio was increased, the length of the stacks of fibrils was also observed to increase. These data demonstrate that a significantly less complex assembly process occurs with the removal of a single carboxylate moiety from the metal binding ligand at the termini of the collagen peptide.

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Self-Assembly of Left- and Right-Handed Molecular Screws

Cited by 57 publications

References 31 publications

Handedness preference and switching of peptide helices. Part I: Helices based on protein amino acids

Handedness preference and switching of peptide helices. Part I: Helices based on protein amino acids

High-resolution structures of a heterochiral coiled coil

Controlling the morphology of metal‐triggered collagen peptide assemblies through ligand alteration

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