Supramolecular helix and β-sheet through self-assembly of two isomeric tetrapeptides in crystals and formation of filaments and ribbons in the solid state

Dutta, Arpita; Dutt, Anita; Drew, Michael G. B.; Pramanik, Animesh

doi:10.1080/10610270701565194

Cited by 14 publications

(8 citation statements)

References 35 publications

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“…4b), as previously reported for other phenyldioxalamates [21,22]. This approach has been used in the determination of conformational changes of peptides [33][34][35] and in the identification of crystal polymorphs [36,37].…”

Section: Ir Spectroscopy Analysismentioning

confidence: 92%

Mechanochemical Complexation of Diethyl N,N´-[1,3-(2-methyl)phenyl]dioxalamate and Resorcinol: Conformational Twist and X-Ray Helical Supramolecular Architecture

González-González¹,

Zúñiga-Lemus²,

Martínez‐Martínez

et al. 2015

J Chem Crystallogr

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The cocrystal formed by diethyl N,Ń -[1,3-(2-methyl)phenyl]dioxalamate (1) and resorcinol (2), namely 1Á2 cryst (C 21 H 24 N 2 O 8 ) was prepared by mechanochemical complexation. IR spectroscopy and powder X-ray diffraction studies allowed to determine the complexation and the conformational switching of the ethyl oxalamate side arms. In the crystal structure of 1Á2 cryst , complexation occurs through O-HÁÁÁO=C hydrogen-bonding interactions with the participation of phenolic O-H as donor and amide carbonyl group as acceptor. The steric hindrance of the CH 3 group in the C-2 position of the aromatic ring leads to a meso-helical supramolecular architecture forming a C 2 2 (16) chain motif. Crystal data: monoclinic, C2/c space group, a = 34.9054(13) Å , b = 8.0434(5) Å , c = 5.1577(8) Å , b = 97.521(3)°. Graphical Abstract The cocrystal formed by diethyl N,Ń -[1,3-(2-methyl)phenyl]dioxalamate and resorcinol, prepared by mechanochemical complexation.

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Section: Ir Spectroscopy Analysismentioning

confidence: 92%

Mechanochemical Complexation of Diethyl N,N´-[1,3-(2-methyl)phenyl]dioxalamate and Resorcinol: Conformational Twist and X-Ray Helical Supramolecular Architecture

González-González¹,

Zúñiga-Lemus²,

Martínez‐Martínez

et al. 2015

J Chem Crystallogr

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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%

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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“…Data collections were performed using φ and ω scans. The structures were solved using direct methods followed by full matrix least-squares refinements against F2 (all data HKLF 4 format) using SHELXTL. − A “Multi-Scan” absorption correction, based on equivalent reflections, was applied to the data. Anisotropic refinement was used for all non-hydrogen atoms.…”

Section: Methodsmentioning

confidence: 99%

“…Supramolecular assemblies are ubiquitous in nature from the perspective of fundamental science. − Over the past few years, several approaches have been devised to stabilize these assemblies using a combination of weak interactions such as hydrogen bonding, electrostatic interactions, π–π interactions, halogen bonding, etc. − However, the reported assemblies are mainly stabilized by backbone interactions of building blocks. − Thus, the design of synthons involving tunable side chain functionalities remains in a rudimentary stage. − …”

Section: Introductionmentioning

confidence: 99%

Can Side Chain Interactions Nucleate Supramolecular Heterogeneity in Synthetic Tripeptides?

Gangele

Goswami

Bar

et al. 2016

Crystal Growth & Design

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In an attempt to artificially imitate the importance of side chains in supramolecular architecture stabilization, we have synthesized a set of four model tripeptides Boc-4(X)-Phe-Aib-Yaa-OMe (I–IV), where X = I, F, N3, and Yaa = Ile/Leu, respectively. Our experimental (X-ray crystallography) and computational investigation (differential functional theory calculations) reveals that the tripeptide (I) self-assembles to form a zigzag ribbon-like assemblage between two conformers, a type III β-turn and an open strand, present in the asymmetric unit. In contrast when a slight modification has been incorporated in the side chains in tripeptides II–IV, it does not support the formation of a ribbon-like organization. Instead, significant heterogeneity is displayed within the supramolecular framework. Interestingly, field emission scanning electron microscopy studies also support the morphological diversities present in the peptides arising due to a mere change of terminal side chains. Thus, the importance of co-operative steric interactions among the side chains of amino acid residues is emphasized in stabilizing a particular supramolecular architecture. This research may not only serve to indicate effective candidates in protein modification but also assist in the rational design of peptidomimetics.

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Supramolecular helix and β-sheet through self-assembly of two isomeric tetrapeptides in crystals and formation of filaments and ribbons in the solid state

Cited by 14 publications

References 35 publications

Mechanochemical Complexation of Diethyl N,N´-[1,3-(2-methyl)phenyl]dioxalamate and Resorcinol: Conformational Twist and X-Ray Helical Supramolecular Architecture

Mechanochemical Complexation of Diethyl N,N´-[1,3-(2-methyl)phenyl]dioxalamate and Resorcinol: Conformational Twist and X-Ray Helical Supramolecular Architecture

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

Can Side Chain Interactions Nucleate Supramolecular Heterogeneity in Synthetic Tripeptides?

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