Studies of β-turn opening with model peptides containing non-coded α-amino isobutyric acid

Dutt, Anita; Dutta, Arpita; Mondal, Raju; Spencer, Elinor C.; Howard, Judith A. K.; Pramanik, Animesh

doi:10.1016/j.tet.2007.07.075

Cited by 25 publications

(15 citation statements)

References 52 publications

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“…The backbone conformation of (I) closely resembles the conformations of several other fully protected tripeptides with a centrally placed Aib residue, e.g. Boc-l-Phe-Aib-l-Ile-OMe (Das et al, 2005), Boc-l-Ile-Aib-l-Val-OMe (Dutt et al, 2007), Boc-l-Ala-Aib-l-Val-OMe (Maji et al, 2004), Boc-l-Ala-Aib-l-Ile-OMe (Maji et al, 2004) and Boc-l-Ala-Aib-l-Ala-OMe, (IV) (Bosch et al, 1984). (IV) crystallizes in the space group P2 1 and forms a distorted -turn with a P II -3 10L -P II backbone conformation very similar to that of (I) (Fig.…”

Section: Commentmentioning

confidence: 59%

N-(tert-Butoxycarbonyl)-O-allyl-L-seryl-α-aminoisobutyryl-L-valine methyl ester: a protected tripeptide with an allylated serine residue

2011

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The title compound [systematic name (6S,12S)-methyl 6-(allyloxymethyl)-12-isopropyl-2,2,9,9-tetramethyl-4,7,10-trioxo-3-oxa-5,8,11-triazatridecan-13-oate], C(21)H(37)N(3)O(7), containing the little studied O-allyl-L-serine residue [Ser(All)], crystallizes in the monoclinic space group C2 with one molecule in the asymmetric unit. The compound is an analogue of the Ser140-Val142 segment of the water channel aquaporin-4 (AQP4). It forms a distorted type-II β-turn with a P(II)-3(10L)-P(II) backbone conformation (P(II) is polyproline II). The overall backbone conformation is markedly different from that of the CO(Pro139)-Val142 stretch of rat AQP4, but is quite similar to the corresponding segment of human AQP4, despite significant differences at the level of the individual residues. The side chain of the Ser(All) residue adopts a gauche conformation relative to the backbone CO-C(α) and C(α)-N bonds. The H atoms of the two CH(2) groups in the Ser(All) side chain are almost eclipsed. The crystal packing of the title compound is divided into one-molecule-thick layers, each layer having a hydrophilic core and distinct hydrophobic interfaces on either side.

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Section: Commentmentioning

confidence: 59%

N-(tert-Butoxycarbonyl)-O-allyl-L-seryl-α-aminoisobutyryl-L-valine methyl ester: a protected tripeptide with an allylated serine residue

2011

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“…Conversely, all the aromatic protons shift upfield as a consequence of π‐π interactions and ring currents exerted by them. In order to determine whether the hydrogen bonds are intra or intermolecular dilution experiments were performed . The NH resonances reveal considerable shifts with change of concentration, suggesting the presence of intermolecular hydrogen bonding within the pseudopeptides.…”

Section: Resultsmentioning

confidence: 99%

“…In recent years short peptide based porous materials are a new entry in this family. Low production cost, biocompatibility, control over structural reversibility and their straightforward chemical synthesis render peptides wonderful platform for biomaterial design . The torsions available in the polypeptide chain often enables peptides an adaptable response to the environment from group of low‐lying and kinetically accessible states.…”

Section: Introductionmentioning

confidence: 99%

Porous Biomaterials via Side Chain‐Side Chain Interactions of Tyrosine Analogue of Pyridine Carboxamides

et al. 2018

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Peptide based porous materials have attracted recent attention due to their environmentally benign nature. In an attempt to artificially imitate their importance, we have synthesized a set of three pseudopeptides comprising of a single pyridinedicarboxylic acid and a flexible dipeptidyl fragment H-Xaa-Yaa-OMe (Xaa: L-Ala, Yaa: mABA, pseudopeptide I ; Xaa: L-Tyr, Yaa : mABA, pseudopeptide II; Xaa: L-Ile, Yaa : Tyr, pseudopeptide III, mABA: meta amino benzoic acid ) using Boc chemistry. Our experimental analysis using X-ray crystallography illustrates that pseudopeptide I-III displays supramolecular preference for double helices, characterestic of pyridine carboxamides, employing intermolecular H-bonding and p-p analogy. To date, literature documentation reveals that the reported double helical motifs have been modulated either by utilizing DNA conjugates or rigid templates, mainly governed by the concept of backbone-backbone interaction. However, to the best of our knowledge these novel examples represent one of the very few reports of the architectural design solely nucleated by ecofriendly amino acids driven by sidechain -sidechain correspondence, exhibiting significant difference in self-assembling properties. Our UV/Visible, concentration dependant NMR experiment and Circular Dichroism measurement complies with the solid state conformational analysis. Interestingly, the double helical ensemble of pseudopeptide II (Tyr analogue bearing additional H-bonding ability of phenolic OH) unveil fifteen times more N 2 sorption (65 cc/g) than pseudopeptide I (Ala, devoid of additional H-bonding ability) (4.5 cc/g), furthermore emphasizing the dominant role of side chain -side chain interaction in porous biomaterial design. Besides our findings also spotlights the relevance of positional displacement of TyrmABA fragment in controlling gas adsorption properties (pseudopeptide III; 5 cc/g). Our morphological analysis using FE-SEM inaddition supports our experimental observation.

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“…The presence of β-sheets may be inferred from a second type of CD spectra. These spectra are of short peptides that adopt a β-turn conformation, with characteristic positive ellipticity between approximately 200 and 235 nm and weak negative ellipticity between 235 and 250 nm in some of the cases [ 57 , 58 ]. Not only does the spectral profile of these peptides resemble the measured spectrum, it has also been reported that such peptides can self-assemble into supramolecular β-sheets and amyloid-like fibrils [ 59 ].…”

Section: Resultsmentioning

confidence: 99%

The Use of the Calcitonin Minimal Recognition Module for the Design of DOPA-Containing Fibrillar Assemblies

et al. 2014

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Amyloid deposits are insoluble fibrous protein aggregates, identified in numerous diseases, which self-assemble through molecular recognition. This process is facilitated by short amino acid sequences, identified as minimal modules. Peptides corresponding to these motifs can be used for the formation of amyloid-like fibrillar assemblies in vitro. Such assemblies hold broad appeal in nanobiotechnology due to their ordered structure and to their ability to be functionalized. The catechol functional group, present in the non-coded L-3,4-dihydroxyphenylalanine (DOPA) amino acid, can take part in diverse chemical interactions. Moreover, DOPA-incorporated polymers have demonstrated adhesive properties and redox activity. In this work, amyloid-like fibrillar assemblies were formed through the self-assembly of a pentapeptide containing DOPA residues, Asp-DOPA-Asn-Lys-DOPA. The design of this peptide was based on the minimal amyloidogenic recognition motif of the human calcitonin hormone, Asp-Phe-Asn-Lys-Phe, the first amyloidogenic pentapeptide identified. By substituting phenylalanine with DOPA, we obtained DOPA-functionalized amyloid-like assemblies in water. Electron microscopy revealed elongated, linear fibril-like nanometric assemblies. Secondary structure analysis indicated the presence of amyloid-characteristic β-sheet structures as well as random coil structures. Deposition of silver on the DOPA-incorporated assemblies suggested redox activity and demonstrated the applicative potential of this novel nanobiomaterial.

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Studies of β-turn opening with model peptides containing non-coded α-amino isobutyric acid

Cited by 25 publications

References 52 publications

N-(tert-Butoxycarbonyl)-O-allyl-L-seryl-α-aminoisobutyryl-L-valine methyl ester: a protected tripeptide with an allylated serine residue

N-(tert-Butoxycarbonyl)-O-allyl-L-seryl-α-aminoisobutyryl-L-valine methyl ester: a protected tripeptide with an allylated serine residue

Porous Biomaterials via Side Chain‐Side Chain Interactions of Tyrosine Analogue of Pyridine Carboxamides

The Use of the Calcitonin Minimal Recognition Module for the Design of DOPA-Containing Fibrillar Assemblies

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