Handedness preference and switching of peptide helices. Part II: Helices based on noncoded<i>α</i>‐amino acids

Crisma, Marco; Zotti, Marta De; Formaggio, Fernando; Peggion, Cristina; Moretto, Alessandro; Toniolo, Claudio

doi:10.1002/psc.2743

Cited by 58 publications

(35 citation statements)

References 440 publications

(684 reference statements)

Supporting

Mentioning

Contrasting

Order By: Relevance

“…In conclusion, the SRCD study performed on several trichogin analogues over the temperature range +20 to −87 °C revealed the occurrence of a reversible, temperature‐driven conformational transition from a right‐ to left‐handed helix promoted by the presence of a C‐terminal methyl ester or free carboxylic acid. Although examples of temperature‐driven screw‐sense helical switch in peptides were previously reported in the literature, this is the first time, to the best of our knowledge, that the promoting effect of a C‐terminal methyl ester (or carboxylic acid) has been unambiguously demonstrated. The involvement of the C‐terminal Aib residue in triggering this switch in Tric‐ol analogues was also proven and confirmed by means of the vT‐NMR study discussed below.…”

Section: Resultsmentioning

confidence: 70%

A Temperature‐Driven, Reversible, Helical‐Handedness Inversion in Peptaibol Analogues Tuned by the C‐Terminal Capping Moiety

et al. 2019

Self Cite

View full text Add to dashboard Cite

Trichogin is a natural peptide endowed with antimicrobial and antitumor activity. A member of the peptaibol family, trichogin possesses a C‐terminal amino alcohol. In the past, this moiety was substituted for a methyl ester for synthetic purposes and it was observed that this apparently slight modification caused significant changes in the peptide bioactivity. With the aim of understanding the reasons behind such observations, a detailed spectroscopic study on a number of trichogin analogues has been performed. Herein, data obtained from synchrotron radiation circular dichroism, NMR spectroscopy, and fluorescence spectroscopy in organic solvents at cryogenic temperatures are compared with those independently acquired by means of EPR spectroscopy at 80 K. It is unambiguously revealed that the presence of a reversible, temperature‐driven, screw‐sense interconversion from a right‐ to left‐handed helix is determined by the C‐terminal capping moiety. Data demonstrate, for the first time, the key role of a C‐terminal methyl ester in promoting peptide screw‐sense inversion.

show abstract

Section: Resultsmentioning

confidence: 70%

A Temperature‐Driven, Reversible, Helical‐Handedness Inversion in Peptaibol Analogues Tuned by the C‐Terminal Capping Moiety

et al. 2019

Self Cite

View full text Add to dashboard Cite

show abstract

“…The α‐amino acids involved range from the by far most commonly found C α ‐ di substituted Gly (Table ) to a very limited number of C α ‐ tri substituted residues, where one example each is provided by the small‐sized representatives Cys, Ala, and Dap (Table ). Moreover, we surprisingly noted a large variety of C α ‐ tetra substituted α‐amino acids (Tables and ), most of them being well known for their extremely effective helicogenic properties . Examples of two derivatives and a very short peptide with an α,β‐didehydro‐α‐amino acid are also given in Table .…”

Section: Detailed Literature Survey On Peptides Since 2012mentioning

confidence: 94%

The fully‐extended conformation in peptides and proteins

et al. 2018

Self Cite

View full text Add to dashboard Cite

The intramolecularly H‐bonded, fully‐extended conformation (C5) of an α‐amino acid residue (and the resulting 2.05‐helix obtained via its propagation) is one of the least extensively investigated types of peptide and protein backbone secondary structure. This situation does still currently occur despite its unique ability to enjoy by far the largest separation per residue among peptide conformations. In this article, we offer a detailed update of our present knowledge on this intriguing 3D‐structure of peptides in the crystal state as obtained from recently published investigations, complemented by a statistical analysis for its occurrence in the crystal structures of α‐amino acid derivatives and peptides available in the Cambridge Structural Database. We have expanded this useful information to the results of a bioinformatics analysis performed on this (so far largely unappreciated) conformation authenticated in all proteins solved by X‐ray diffraction to a resolution of ≤ 1.5 Å. In the last section, we describe the results of our DFT calculations on the conformational preferences of a set of homopeptides (from monomer to octamer) based on as many as six proteins and two noncoded, carefully selected, α‐amino acids. From this literature survey integrated by new energy calculations, we have definitely provided strong support to the thesis that this polypeptide 3D‐structure does indeed exist, it should be not neglected in future studies by structural biochemists, and it represents a very attractive, novel backbone for applications for organic, medicinal, and biomaterials chemists.

show abstract

“…[1][2][3][4][5][6] As a dAA, α-aminoisobutyric acid (Aib) has widely been used to induce helical structures. A right-handed (P) 3 10 -helix is induced in relatively shorter L-amino acid-based peptides having a high Aib content; however, a right-handed (P) α-helix is preferentially formed in relatively longer L-amino acid-based peptides having a low Aib content.…”

Section: Introductionmentioning

confidence: 99%

Helical l–Leu‐Based Peptides Having Chiral Five‐Membered Carbocyclic Ring Amino Acids with an Ethylene Acetal Moiety

et al. 2017

View full text Add to dashboard Cite

L-Leu-based heteropeptides having (R)-or (S)-chiral five-membered carbocyclic ring amino acids (Ac 5 c 3EG ) with an ethylene acetal moiety were prepared. A conformational analysis using FT-IR absorption, 1 H NMR, and CD spectra revealed that L-Leu-based hexapeptides and nonapeptides having (R)-or (S)-Ac 5 c 3EG formed right-handed (P) helical structures in solution. An X-ray crystallographic analysis of nonapeptides 5a and 5b showed similar right-handed (P) α-helical structures, without an intramolecular hydrogen bond of the peptide N-H···-O-(acetal) type.

show abstract

Handedness preference and switching of peptide helices. Part II: Helices based on noncodedα‐amino acids

Cited by 58 publications

References 440 publications

A Temperature‐Driven, Reversible, Helical‐Handedness Inversion in Peptaibol Analogues Tuned by the C‐Terminal Capping Moiety

A Temperature‐Driven, Reversible, Helical‐Handedness Inversion in Peptaibol Analogues Tuned by the C‐Terminal Capping Moiety

The fully‐extended conformation in peptides and proteins

Helical l–Leu‐Based Peptides Having Chiral Five‐Membered Carbocyclic Ring Amino Acids with an Ethylene Acetal Moiety

Contact Info

Product

Resources

About