Conformationally restricted amino acids and dipeptides, (non)peptidomimetics and secondary structure mimetics

Liskamp, Rob M. J.

doi:10.1002/recl.19941130102

Cited by 181 publications

(7 citation statements)

References 140 publications

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“…Boc‐ l ‐Leu‐Aib‐Aib‐Aib‐Aib‐ l ‐Leu‐OMe ( 1a ) is crystallized in space group P 2 1 to form a right‐handed ( P ) 3 10 ‐helix (Figure ). The mean values of the ϕ and ψ torsion angles of the amino acid residues (1–6) were −60.1° and −27.9°, respectively, which are close to those for an ideal right‐handed ( P ) 3 10 ‐helical structure (−60° and −30°) . Four intramolecular hydrogen bonds, which each form a 10‐membered (atoms) pseudo ring of the i ← i + 3 type, exist in the 3 10 ‐helical molecule of 1a .…”

Section: Resultssupporting

confidence: 53%

Conformations of helical Aib peptides containing a pair of l‐amino acid and d‐amino acid

Demizu

Yabuki

Doi

et al. 2012

Journal of Peptide Science

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A pair of L-leucine (L-Leu) and D-leucine (D-Leu) was incorporated into a-aminoisobutyric acid (Aib) peptide segments. Thedominant conformations of four hexapeptides, Boc-L-Leu-Aib-Aib-Aib-Aib-L-Leu-OMe (1a), Boc-D-Leu-Aib-Aib-Aib-Aib-L-Leu-OMe(1b), Boc-Aib-Aib-L-Leu-L-Leu-Aib-Aib-OMe (2a), and Boc-Aib-Aib-D-Leu-L-Leu-Aib-Aib-OMe (2b), were investigated by IR,¹H NMR, CD spectra, and X-ray crystallographic analysis. All peptides 1a,b and 2a,b formed 3₁₀-helical structures in solution. X-ray crystallographic analysis revealed that right-handed (P) 3₁₀-helices were present in 1a and 1b and a mixture of right-handed(P) and left-handed (M) 3₁₀-helices was present in 2b in their crystalline states.

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Section: Resultssupporting

confidence: 53%

Conformations of helical Aib peptides containing a pair of l‐amino acid and d‐amino acid

Demizu

Yabuki

Doi

et al. 2012

Journal of Peptide Science

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“…The average φ and ψ torsion angles of residues (1-8) were -61.6° and -44.7°, respectively, which were consistent with those of the ideal (P) α-helix (−57° and −47°). [30][31][32][33] However, the signs of the φ and ψ torsion angles of the (S)-Ac 6 c 3EG residue (9) at the C-terminus were positive, and opposite to those of the preceding residues. The reversal of the signs of the C-terminal residue torsion angles are frequently observed in helical Aib and related peptides, and known as the helix-terminating structure.…”

Section: Conformational Analysis In Solutionmentioning

confidence: 93%

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

et al. 2017

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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.

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“…This approach is based on enhancing the bioavailability and activity of native peptides and proteins, which are considered as tools to develop drug candidates and new therapeutic classes, by introducing both functional and structural specific modifications while maintaining main features responsible for biological activity [ 21 ]. Apart from displaying greater oral bioavailability and biological activity, peptidomimetics may also show high cell selectivity than native peptides [ 23 , 24 ]. Peptidomimetics are divided into three classes depending on their functional and structural characteristics and these include [ 25 ]: Class I (structural mimetics): show a structural analogy with the native substrate in a well- defined spatial orientation, they carry all the functionalities responsible for the interaction with a receptor or an enzyme.…”

Section: Introductionmentioning

confidence: 99%

Antimicrobial and Antibiofilm Activity of UP-5, an Ultrashort Antimicrobial Peptide Designed Using Only Arginine and Biphenylalanine

et al. 2018

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The recent upsurge of multidrug resistant bacteria (MDRB) among global communities has become one of the most serious challenges facing health professionals and the human population worldwide. Cationic ultrashort antimicrobial peptides (USAMPs) are a promising group of molecules that meet the required criteria of novel antimicrobial drug development. UP-5, a novel penta-peptide, displayed significant antimicrobial activities against various standard and clinical isolates of MDRB. UP-5 displayed MICs values within the range of (10–15 μM) and (55–65 μM) against Gram-positive and Gram-negative bacteria, respectively. Furthermore, UP-5 displayed antibiofilm activity with minimum biofilm eradication concentration (MBEC) value as equal to twofold higher than MIC value. At the same inhibitory concentrations, UP-5 exhibited very low or negligible toxicity toward human erythrocytes and mammalian cells. Combining UP-5 with conventional antibiotics led to a synergistic or additive mode of action that resulted in the reduction of the MIC values for some of the antibiotics by 99.7% along a significant drop in MIC values of the peptide. The stability profile of UP-5 was evaluated in full mouse plasma and serum with results indicating a more stable pattern in plasma. The present study indicates that USAMPs are promising antimicrobial agents that can avoid the negative characteristics of conventional antimicrobial peptides. Additionally, USAMPs exhibit good to moderate activity against MDRB, negligible toxicity, and synergistic outcomes in combination with conventional antimicrobial agents.

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Conformationally restricted amino acids and dipeptides, (non)peptidomimetics and secondary structure mimetics

Abstract: Reciieil cles

Cited by 181 publications

References 140 publications

Conformations of helical Aib peptides containing a pair of l‐amino acid and d‐amino acid

Conformations of helical Aib peptides containing a pair of l‐amino acid and d‐amino acid

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

Antimicrobial and Antibiofilm Activity of UP-5, an Ultrashort Antimicrobial Peptide Designed Using Only Arginine and Biphenylalanine

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