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Showing 1 to 12 of 81 entries
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Solution structure of the anticancer p28 peptide in biomimetic medium.

Journal of peptide science : an official publication of the European Peptide Society

Cantini F, Gianni' P, Savarin P, Bizzarri AR, Sette M.
PMID: 34151482
J Pept Sci. 2021 Nov;27(11):e3357. doi: 10.1002/psc.3357. Epub 2021 Jun 20.

The p28 peptide derived from Pseudomonas aeruginosa azurin shows an anticancer activity after binding to p53 protein and is currently in Phase I of clinical trials. We have studied its structure in water and in a biomimetic media and...

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Cantini F, Gianni' P, Savarin P, et al. Solution structure of the anticancer p28 peptide in biomimetic medium. J Pept Sci. 2021;27(11):e3357doi: 10.1002/psc.3357.
Cantini, F., Gianni', P., Savarin, P., Bizzarri, A. R., & Sette, M. (2021). Solution structure of the anticancer p28 peptide in biomimetic medium. Journal of peptide science : an official publication of the European Peptide Society, 27(11), e3357. https://doi.org/10.1002/psc.3357
Cantini, Francesca, et al. "Solution structure of the anticancer p28 peptide in biomimetic medium." Journal of peptide science : an official publication of the European Peptide Society vol. 27,11 (2021): e3357. doi: https://doi.org/10.1002/psc.3357
Cantini F, Gianni' P, Savarin P, Bizzarri AR, Sette M. Solution structure of the anticancer p28 peptide in biomimetic medium. J Pept Sci. 2021 Nov;27(11):e3357. doi: 10.1002/psc.3357. Epub 2021 Jun 20. PMID: 34151482.
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Biophysical study of the structure and dynamics of the antimicrobial peptide maximin 1.

Journal of peptide science : an official publication of the European Peptide Society

Timmons PB, Hewage CM.
PMID: 34569121
J Pept Sci. 2022 Feb;28(2):e3370. doi: 10.1002/psc.3370. Epub 2021 Sep 26.

Maximin 1 is a cationic, amphipathic antimicrobial peptide found in the skin secretions and brains of the Chinese red belly toad Bombina maxima. The 27 amino acid residue-long peptide is biologically interesting as it possesses a variety of biological...

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Timmons PB, Hewage CM. Biophysical study of the structure and dynamics of the antimicrobial peptide maximin 1. J Pept Sci. 2021;28(2):e3370doi: 10.1002/psc.3370.
Timmons, P. B., & Hewage, C. M. (2022). Biophysical study of the structure and dynamics of the antimicrobial peptide maximin 1. Journal of peptide science : an official publication of the European Peptide Society, 28(2), e3370. https://doi.org/10.1002/psc.3370
Timmons, Patrick B, and Hewage, Chandralal M. "Biophysical study of the structure and dynamics of the antimicrobial peptide maximin 1." Journal of peptide science : an official publication of the European Peptide Society vol. 28,2 (2022): e3370. doi: https://doi.org/10.1002/psc.3370
Timmons PB, Hewage CM. Biophysical study of the structure and dynamics of the antimicrobial peptide maximin 1. J Pept Sci. 2022 Feb;28(2):e3370. doi: 10.1002/psc.3370. Epub 2021 Sep 26. PMID: 34569121.
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The life and work of Robert (Bob) C. Sheppard.

Journal of peptide science : an official publication of the European Peptide Society

Wade JD, Jones JH.
PMID: 34611959
J Pept Sci. 2022 Feb;28(2):e3369. doi: 10.1002/psc.3369. Epub 2021 Oct 05.

The life and work of Robert Charles Sheppard (1932-2019), Bob Sheppard informally among friends, is outlined. He was a leading pioneer of solid phase peptide synthesis and made the most significant and fundamental European contribution to the art of...

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Wade JD, Jones JH. The life and work of Robert (Bob) C. Sheppard. J Pept Sci. 2021;28(2):e3369doi: 10.1002/psc.3369.
Wade, J. D., & Jones, J. H. (2022). The life and work of Robert (Bob) C. Sheppard. Journal of peptide science : an official publication of the European Peptide Society, 28(2), e3369. https://doi.org/10.1002/psc.3369
Wade, John D, and Jones, John H. "The life and work of Robert (Bob) C. Sheppard." Journal of peptide science : an official publication of the European Peptide Society vol. 28,2 (2022): e3369. doi: https://doi.org/10.1002/psc.3369
Wade JD, Jones JH. The life and work of Robert (Bob) C. Sheppard. J Pept Sci. 2022 Feb;28(2):e3369. doi: 10.1002/psc.3369. Epub 2021 Oct 05. PMID: 34611959.
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Effects of N-terminal modifications on the stability of antimicrobial peptide SAMP-A4 analogues against protease degradation.

Journal of peptide science : an official publication of the European Peptide Society

Li R, He S, Yin K, Zhang B, Yi Y, Zhang M, Pei N, Huang L.
PMID: 34028137
J Pept Sci. 2021 Oct;27(10):e3352. doi: 10.1002/psc.3352. Epub 2021 May 24.

Infections with multidrug-resistant (MDR) pathogens are increasingly concerning for public health. Synthesized antimicrobial peptide A4 (SAMP-A4), a peptide computationally designed by our research team, is a potential drug candidate. However, the antimicrobial peptide SAMP-A4 is easily degraded in serum....

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Li R, He S, Yin K, et al. Effects of N-terminal modifications on the stability of antimicrobial peptide SAMP-A4 analogues against protease degradation. J Pept Sci. 2021;27(10):e3352doi: 10.1002/psc.3352.
Li, R., He, S., Yin, K., Zhang, B., Yi, Y., Zhang, M., Pei, N., & Huang, L. (2021). Effects of N-terminal modifications on the stability of antimicrobial peptide SAMP-A4 analogues against protease degradation. Journal of peptide science : an official publication of the European Peptide Society, 27(10), e3352. https://doi.org/10.1002/psc.3352
Li, Ruifang, et al. "Effects of N-terminal modifications on the stability of antimicrobial peptide SAMP-A4 analogues against protease degradation." Journal of peptide science : an official publication of the European Peptide Society vol. 27,10 (2021): e3352. doi: https://doi.org/10.1002/psc.3352
Li R, He S, Yin K, Zhang B, Yi Y, Zhang M, Pei N, Huang L. Effects of N-terminal modifications on the stability of antimicrobial peptide SAMP-A4 analogues against protease degradation. J Pept Sci. 2021 Oct;27(10):e3352. doi: 10.1002/psc.3352. Epub 2021 May 24. PMID: 34028137.
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Intracellular targets: A multiple cargo transporting molecule.

Journal of peptide science : an official publication of the European Peptide Society

Papadopoulos C, Fotou E, Moussis V, Ntoyhaniari A, Zografou S, Maltabe V, Kouklis P, Christoforidis S, Tsikaris V.
PMID: 34131994
J Pept Sci. 2021 Nov;27(11):e3359. doi: 10.1002/psc.3359. Epub 2021 Jun 15.

The generation of cell-penetrating peptides as cargo-delivery systems has produced an immense number of studies owing to the importance of these systems as tools to deliver molecules into the cells, as well as due to the interest to shed...

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Papadopoulos C, Fotou E, Moussis V, et al. Intracellular targets: A multiple cargo transporting molecule. J Pept Sci. 2021;27(11):e3359doi: 10.1002/psc.3359.
Papadopoulos, C., Fotou, E., Moussis, V., Ntoyhaniari, A., Zografou, S., Maltabe, V., Kouklis, P., Christoforidis, S., & Tsikaris, V. (2021). Intracellular targets: A multiple cargo transporting molecule. Journal of peptide science : an official publication of the European Peptide Society, 27(11), e3359. https://doi.org/10.1002/psc.3359
Papadopoulos, Christos, et al. "Intracellular targets: A multiple cargo transporting molecule." Journal of peptide science : an official publication of the European Peptide Society vol. 27,11 (2021): e3359. doi: https://doi.org/10.1002/psc.3359
Papadopoulos C, Fotou E, Moussis V, Ntoyhaniari A, Zografou S, Maltabe V, Kouklis P, Christoforidis S, Tsikaris V. Intracellular targets: A multiple cargo transporting molecule. J Pept Sci. 2021 Nov;27(11):e3359. doi: 10.1002/psc.3359. Epub 2021 Jun 15. PMID: 34131994.
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Effect of the powerful plasticity of the tert-butyl side chain on the conformational equilibrium of ascidiacyclamides.

Journal of peptide science : an official publication of the European Peptide Society

Asano A, Nakagawa M, Miyajima C, Yasui M, Minoura K, Yamada T, Doi M.
PMID: 34462993
J Pept Sci. 2021 Dec;27(12):e3363. doi: 10.1002/psc.3363. Epub 2021 Aug 30.

Ascidiacyclamide [cyclo(-Ile

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Asano A, Nakagawa M, Miyajima C, et al. Effect of the powerful plasticity of the tert-butyl side chain on the conformational equilibrium of ascidiacyclamides. J Pept Sci. 2021;27(12):e3363doi: 10.1002/psc.3363.
Asano, A., Nakagawa, M., Miyajima, C., Yasui, M., Minoura, K., Yamada, T., & Doi, M. (2021). Effect of the powerful plasticity of the tert-butyl side chain on the conformational equilibrium of ascidiacyclamides. Journal of peptide science : an official publication of the European Peptide Society, 27(12), e3363. https://doi.org/10.1002/psc.3363
Asano, Akiko, et al. "Effect of the powerful plasticity of the tert-butyl side chain on the conformational equilibrium of ascidiacyclamides." Journal of peptide science : an official publication of the European Peptide Society vol. 27,12 (2021): e3363. doi: https://doi.org/10.1002/psc.3363
Asano A, Nakagawa M, Miyajima C, Yasui M, Minoura K, Yamada T, Doi M. Effect of the powerful plasticity of the tert-butyl side chain on the conformational equilibrium of ascidiacyclamides. J Pept Sci. 2021 Dec;27(12):e3363. doi: 10.1002/psc.3363. Epub 2021 Aug 30. PMID: 34462993.
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DIC/Oxyma-based accelerated synthesis and oxidative folding studies of centipede toxin RhTx.

Journal of peptide science : an official publication of the European Peptide Society

Chen XT, Wang JY, Ma YN, Dong LY, Jia SX, Yin H, Fu XY, Du SS, Qi YK, Wang K.
PMID: 34514664
J Pept Sci. 2021 Sep 12;e3368. doi: 10.1002/psc.3368. Epub 2021 Sep 12.

Coupling reagents play crucial roles in the iterative construction of amide bonds for the synthesis of peptides and peptide-based derivatives. The novel DIC/Oxyma condensation system featured with the low risk of explosion displayed remarkable abilities to inhibit racemization, along...

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Chen XT, Wang JY, Ma YN, et al. DIC/Oxyma-based accelerated synthesis and oxidative folding studies of centipede toxin RhTx. J Pept Sci. 2021;e3368doi: 10.1002/psc.3368.
Chen, X. T., Wang, J. Y., Ma, Y. N., Dong, L. Y., Jia, S. X., Yin, H., Fu, X. Y., Du, S. S., Qi, Y. K., & Wang, K. (2021). DIC/Oxyma-based accelerated synthesis and oxidative folding studies of centipede toxin RhTx. Journal of peptide science : an official publication of the European Peptide Society, e3368. https://doi.org/10.1002/psc.3368
Chen, Xi-Tong, et al. "DIC/Oxyma-based accelerated synthesis and oxidative folding studies of centipede toxin RhTx." Journal of peptide science : an official publication of the European Peptide Society vol. (2021): e3368. doi: https://doi.org/10.1002/psc.3368
Chen XT, Wang JY, Ma YN, Dong LY, Jia SX, Yin H, Fu XY, Du SS, Qi YK, Wang K. DIC/Oxyma-based accelerated synthesis and oxidative folding studies of centipede toxin RhTx. J Pept Sci. 2021 Sep 12;e3368. doi: 10.1002/psc.3368. Epub 2021 Sep 12. PMID: 34514664.
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Peptide hydrogels for affinity-controlled release of therapeutic cargo: Current and potential strategies.

Journal of peptide science : an official publication of the European Peptide Society

Nambiar M, Schneider JP.
PMID: 34747114
J Pept Sci. 2022 Jan;28(1):e3377. doi: 10.1002/psc.3377. Epub 2021 Nov 07.

The development of devices for the precise and controlled delivery of therapeutics has grown rapidly over the last few decades. Drug delivery materials must provide a depot with delivery profiles that satisfy pharmacodynamic and pharmacokinetic requirements resulting in clinical...

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Nambiar M, Schneider JP. Peptide hydrogels for affinity-controlled release of therapeutic cargo: Current and potential strategies. J Pept Sci. 2021;28(1):e3377doi: 10.1002/psc.3377.
Nambiar, M., & Schneider, J. P. (2022). Peptide hydrogels for affinity-controlled release of therapeutic cargo: Current and potential strategies. Journal of peptide science : an official publication of the European Peptide Society, 28(1), e3377. https://doi.org/10.1002/psc.3377
Nambiar, Monessha, and Schneider, Joel P. "Peptide hydrogels for affinity-controlled release of therapeutic cargo: Current and potential strategies." Journal of peptide science : an official publication of the European Peptide Society vol. 28,1 (2022): e3377. doi: https://doi.org/10.1002/psc.3377
Nambiar M, Schneider JP. Peptide hydrogels for affinity-controlled release of therapeutic cargo: Current and potential strategies. J Pept Sci. 2022 Jan;28(1):e3377. doi: 10.1002/psc.3377. Epub 2021 Nov 07. PMID: 34747114; PMCID: PMC8678354.
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Current synthetic chemistry towards cyclic antimicrobial peptides.

Journal of peptide science : an official publication of the European Peptide Society

He T, Qu R, Zhang J.
PMID: 34931393
J Pept Sci. 2021 Dec 21;e3387. doi: 10.1002/psc.3387. Epub 2021 Dec 21.

Antimicrobial peptides (AMPs) have great potentials for developing novel antibiotics against multi-drug resistant (MDR) bacteria. However, the clinical application of AMPs is limited due to their poor protease stability and high hemolytic toxicity. Various strategies have been widely explored...

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He T, Qu R, Zhang J. Current synthetic chemistry towards cyclic antimicrobial peptides. J Pept Sci. 2021;e3387doi: 10.1002/psc.3387.
He, T., Qu, R., & Zhang, J. (2021). Current synthetic chemistry towards cyclic antimicrobial peptides. Journal of peptide science : an official publication of the European Peptide Society, e3387. https://doi.org/10.1002/psc.3387
He, Tong, et al. "Current synthetic chemistry towards cyclic antimicrobial peptides." Journal of peptide science : an official publication of the European Peptide Society vol. (2021): e3387. doi: https://doi.org/10.1002/psc.3387
He T, Qu R, Zhang J. Current synthetic chemistry towards cyclic antimicrobial peptides. J Pept Sci. 2021 Dec 21;e3387. doi: 10.1002/psc.3387. Epub 2021 Dec 21. PMID: 34931393.
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Substrate plasticity of dehydratase SpaKC from the biosynthesis of thiosparsoamide.

Journal of peptide science : an official publication of the European Peptide Society

Wang C, Lu J, Zhang Y, Zheng J, Sun S, Huang S, Wang H.
PMID: 34931400
J Pept Sci. 2021 Dec 20;e3388. doi: 10.1002/psc.3388. Epub 2021 Dec 20.

Thioamitides are a group of ribosomally synthesized and post-translationally modified peptides that possess diverse bioactivities and are usually featured by thioamide and 2-aminovinyl-cysteine (AviCys) motifs. In natural product thiosparsoamide, the AviCys motif is formed by an enzyme cascade formed...

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Wang C, Lu J, Zhang Y, et al. Substrate plasticity of dehydratase SpaKC from the biosynthesis of thiosparsoamide. J Pept Sci. 2021;e3388doi: 10.1002/psc.3388.
Wang, C., Lu, J., Zhang, Y., Zheng, J., Sun, S., Huang, S., & Wang, H. (2021). Substrate plasticity of dehydratase SpaKC from the biosynthesis of thiosparsoamide. Journal of peptide science : an official publication of the European Peptide Society, e3388. https://doi.org/10.1002/psc.3388
Wang, Ciji, et al. "Substrate plasticity of dehydratase SpaKC from the biosynthesis of thiosparsoamide." Journal of peptide science : an official publication of the European Peptide Society vol. (2021): e3388. doi: https://doi.org/10.1002/psc.3388
Wang C, Lu J, Zhang Y, Zheng J, Sun S, Huang S, Wang H. Substrate plasticity of dehydratase SpaKC from the biosynthesis of thiosparsoamide. J Pept Sci. 2021 Dec 20;e3388. doi: 10.1002/psc.3388. Epub 2021 Dec 20. PMID: 34931400.
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Structure-activity relationship study of amphipathic antimicrobial peptides using helix-destabilizing sarcosine.

Journal of peptide science : an official publication of the European Peptide Society

Yokoo H, Hirano M, Ohoka N, Misawa T, Demizu Y.
PMID: 34164880
J Pept Sci. 2021 Dec;27(12):e3360. doi: 10.1002/psc.3360. Epub 2021 Jun 23.

Antimicrobial peptides (AMPs) are potential therapeutic agents against bacteria. We recently showed that a rationally designed AMP, termed Stripe, with an amphipathic distribution of native cationic and hydrophobic amino acids on its helical structure exhibited potent antimicrobial activity against...

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Yokoo H, Hirano M, Ohoka N, et al. Structure-activity relationship study of amphipathic antimicrobial peptides using helix-destabilizing sarcosine. J Pept Sci. 2021;27(12):e3360doi: 10.1002/psc.3360.
Yokoo, H., Hirano, M., Ohoka, N., Misawa, T., & Demizu, Y. (2021). Structure-activity relationship study of amphipathic antimicrobial peptides using helix-destabilizing sarcosine. Journal of peptide science : an official publication of the European Peptide Society, 27(12), e3360. https://doi.org/10.1002/psc.3360
Yokoo, Hidetomo, et al. "Structure-activity relationship study of amphipathic antimicrobial peptides using helix-destabilizing sarcosine." Journal of peptide science : an official publication of the European Peptide Society vol. 27,12 (2021): e3360. doi: https://doi.org/10.1002/psc.3360
Yokoo H, Hirano M, Ohoka N, Misawa T, Demizu Y. Structure-activity relationship study of amphipathic antimicrobial peptides using helix-destabilizing sarcosine. J Pept Sci. 2021 Dec;27(12):e3360. doi: 10.1002/psc.3360. Epub 2021 Jun 23. PMID: 34164880.
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Virtual screening and rational design of antioxidant peptides based on tryptophyllin L structures isolated from the Litoria rubella frog.

Journal of peptide science : an official publication of the European Peptide Society

Tran TTN, Tran DP, Nguyen TMA, Tran TH, Phan NNA, Nguyen VC, Nguyen VT, Bowie JH.
PMID: 34779094
J Pept Sci. 2021 Nov 14;e3380. doi: 10.1002/psc.3380. Epub 2021 Nov 14.

Discovery of natural antioxidants has been carried out for decades relying mainly on experimental approaches that are commonly associated with time and cost demanding biochemical assays. The maturation of quantitative structure activity relationship (QSAR) modelling has provided an alternative...

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Tran TTN, Tran DP, Nguyen TMA, et al. Virtual screening and rational design of antioxidant peptides based on tryptophyllin L structures isolated from the Litoria rubella frog. J Pept Sci. 2021;e3380doi: 10.1002/psc.3380.
Tran, T. T. N., Tran, D. P., Nguyen, T. M. A., Tran, T. H., Phan, N. N. A., Nguyen, V. C., Nguyen, V. T., & Bowie, J. H. (2021). Virtual screening and rational design of antioxidant peptides based on tryptophyllin L structures isolated from the Litoria rubella frog. Journal of peptide science : an official publication of the European Peptide Society, e3380. https://doi.org/10.1002/psc.3380
Tran, Thi Thanh Nha, et al. "Virtual screening and rational design of antioxidant peptides based on tryptophyllin L structures isolated from the Litoria rubella frog." Journal of peptide science : an official publication of the European Peptide Society vol. (2021): e3380. doi: https://doi.org/10.1002/psc.3380
Tran TTN, Tran DP, Nguyen TMA, Tran TH, Phan NNA, Nguyen VC, Nguyen VT, Bowie JH. Virtual screening and rational design of antioxidant peptides based on tryptophyllin L structures isolated from the Litoria rubella frog. J Pept Sci. 2021 Nov 14;e3380. doi: 10.1002/psc.3380. Epub 2021 Nov 14. PMID: 34779094.
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Showing 1 to 12 of 81 entries