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2,668 results on '"Craik, David J."'

164. An Ultrapotent and Selective Cyclic Peptide Inhibitor of Human β-Factor XIIa in a Cyclotide Scaffold

Author

Liu, Wenyu, primary, de Veer, Simon J., additional, Huang, Yen-Hua, additional, Sengoku, Toru, additional, Okada, Chikako, additional, Ogata, Kazuhiro, additional, Zdenek, Christina N., additional, Fry, Bryan G., additional, Swedberg, Joakim E., additional, Passioura, Toby, additional, Craik, David J., additional, and Suga, Hiroaki, additional

Published
2021
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176. Melanocortin 1 Receptor Agonists Based on a Bivalent, Bicyclic Peptide Framework

Author

Durek, Thomas, primary, Kaas, Quentin, additional, White, Andrew M., additional, Weidmann, Joachim, additional, Fuaad, Abdullah Ahmad, additional, Cheneval, Olivier, additional, Schroeder, Christina I., additional, de Veer, Simon J., additional, Dellsén, Anita, additional, Österlund, Torben, additional, Larsson, Niklas, additional, Knerr, Laurent, additional, Bauer, Udo, additional, Plowright, Alleyn T., additional, and Craik, David J., additional

Published
2021
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177. Modified defence peptides from horseshoe crab target and kill bacteria inside host cells

Author

Amiss, Anna S., primary, von Pein, Jessica B., additional, Webb, Jessica R., additional, Condon, Nicholas D., additional, Harvey, Peta J., additional, Phan, Minh-Duy, additional, Schembri, Mark A., additional, Currie, Bart J., additional, Sweet, Matthew J., additional, Craik, David J., additional, Kapetanovic, Ronan, additional, Henriques, Sónia Troeira, additional, and Lawrence, Nicole, additional

Published
2021
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178. Design of a Stable Cyclic Peptide Analgesic Derived from Sunflower Seeds that Targets the κ-Opioid Receptor for the Treatment of Chronic Abdominal Pain

Author

Muratspahić, Edin, primary, Tomašević, Nataša, additional, Koehbach, Johannes, additional, Duerrauer, Leopold, additional, Hadžić, Seid, additional, Castro, Joel, additional, Schober, Gudrun, additional, Sideromenos, Spyridon, additional, Clark, Richard J., additional, Brierley, Stuart M., additional, Craik, David J., additional, and Gruber, Christian W., additional

Published
2021
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182. Salt-Tolerant antifungal and antibacterial activities of the corn defensin ZmD32

Author

Bomai K Kerenga, McKenna, James, Harvey, Peta J, Dominguez, Pedro Quimbar, Garcia-Ceron, Donovan, Fung Lay, Phan, Thanh, Veneer, Prem, Shaily Vasa, Parisi, Kathy, Shafee, Thomas, Weerden, Nicole Van Der, Hulett, Mark, Craik, David J, Anderson, Marilyn, and Bleackley, Mark

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Abstract

Copyright © 2019 Kerenga, McKenna, Harvey, Quimbar, Garcia-Ceron, Lay, Phan, Veneer, Vasa, Parisi, Shafee, van der Weerden, Hulett, Craik, Anderson and Bleackley. This is an open-access article distributed under the terms of the Creative Commons Attribution License (CC BY). The use, distribution or reproduction in other forums is permitted, provided the original author(s) and the copyright owner(s) are credited and that the original publication in this journal is cited, in accordance with accepted academic practice. No use, distribution or reproduction is permitted which does not comply with these terms. Pathogenic microbes are developing resistance to established antibiotics, making the development of novel antimicrobial molecules paramount. One major resource for discovery of antimicrobials is the arsenal of innate immunity molecules that are part of the first line of pathogen defense in many organisms. Gene encoded cationic antimicrobial peptides are a major constituent of innate immune arsenals. Many of these peptides exhibit potent antimicrobial activity in vitro. However, a major hurdle that has impeded their development for use in the clinic is the loss of activity at physiological salt concentrations, attributed to weakening of the electrostatic interactions between the cationic peptide and anionic surfaces of the microbial cells in the presence of salt. Using plant defensins we have investigated the relationship between the charge of an antimicrobial peptide and its activity in media with elevated salt concentrations. Plant defensins are a large class of antifungal peptides that have remarkable stability at extremes of pH and temperature as well as resistance to protease digestion. A search of a database of over 1200 plant defensins identified ZmD32, a defensin from Zea mays, with a predicted charge of +10.1 at pH 7, the highest of any defensin in the database. Recombinant ZmD32 retained activity against a range of fungal species in media containing elevated concentrations of salt. In addition, ZmD32 was active against Candida albicans biofilms as well as both Gram negative and Gram-positive bacteria. This broad spectrum antimicrobial activity, combined with a low toxicity on human cells make ZmD32 an attractive lead for development of future antimicrobial molecules.

Published
2021
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183. Cyclic gomesin, a stable redesigned spider peptide able to enter cancer cells

Author

Benfield, Aurélie H., Defaus, Sira, Lawrence, Nicole, Chaousis, Stephanie, Condon, Nicholas, Cheneval, Olivier, Huang, Yen Hua, Chan, Lai Yue, Andreu, David, Craik, David J., Henriques, Sónia Troeira, Benfield, Aurélie H., Defaus, Sira, Lawrence, Nicole, Chaousis, Stephanie, Condon, Nicholas, Cheneval, Olivier, Huang, Yen Hua, Chan, Lai Yue, Andreu, David, Craik, David J., and Henriques, Sónia Troeira

Abstract

Anticancer chemo- and targeted therapies are limited in some cases due to strong side effects and/or drug resistance. Peptides have received renascent interest as anticancer therapeutics and are currently being considered as alternatives and/or as complementary to biologics and small-molecule drugs. Gomesin, a disulfide-rich host defense peptide expressed in the Brazilian spider Acanthoscurria gomesiana selectively targets and disrupts cancer cell membranes. In the current study, we employed a range of biophysical methodologies with model membranes and bioassays to investigate the use of a cyclic analogue of gomesin as a drug scaffold to internalize cancer cells. We found that cyclic gomesin can internalize cancer cells via endocytosis and direct membrane permeation. In addition, we designed an improved non-disruptive and non-toxic cyclic gomesin analogue by incorporating D-amino acids within the scaffold. This improved analogue retained the ability to enter cancer cells and can be used as a scaffold to deliver drugs. Efforts to investigate the internalization mechanism used by host defense peptides, and to improve their stability, potency, selectivity and ability to permeate cancer cell membranes will increase the opportunities to repurpose peptides as templates for designing alternative anticancer therapeutic leads.

Published
2021

184. Short Cationic Peptide Derived from Archaea with Dual Antibacterial Properties and Anti-Infective Potential

Author

Massachusetts Institute of Technology. Synthetic Biology Center, Massachusetts Institute of Technology. Center for Microbiome Informatics and Therapeutics, Massachusetts Institute of Technology. Research Laboratory of Electronics, Massachusetts Institute of Technology. Department of Biological Engineering, Massachusetts Institute of Technology. Department of Electrical Engineering and Computer Science, Cândido, Elizabete S, Cardoso, Marlon H, Chan, Lai Y, Torres, Marcelo DT, Oshiro, Karen GN, Porto, William F, Ribeiro, Suzana M, Haney, Evan F, Hancock, Robert EW, Lu, Timothy K, de la Fuente-Nunez, Cesar, Craik, David J, Franco, Octávio L, Massachusetts Institute of Technology. Synthetic Biology Center, Massachusetts Institute of Technology. Center for Microbiome Informatics and Therapeutics, Massachusetts Institute of Technology. Research Laboratory of Electronics, Massachusetts Institute of Technology. Department of Biological Engineering, Massachusetts Institute of Technology. Department of Electrical Engineering and Computer Science, Cândido, Elizabete S, Cardoso, Marlon H, Chan, Lai Y, Torres, Marcelo DT, Oshiro, Karen GN, Porto, William F, Ribeiro, Suzana M, Haney, Evan F, Hancock, Robert EW, Lu, Timothy K, de la Fuente-Nunez, Cesar, Craik, David J, and Franco, Octávio L

Abstract

Copyright © 2019 American Chemical Society. Bacterial biofilms and associated infections represent one of the biggest challenges in the clinic, and as an alternative to counter bacterial infections, antimicrobial peptides have attracted great attention in the past decade. Here, ten short cationic antimicrobial peptides were generated through a sliding-window strategy on the basis of the 19-amino acid residue peptide, derived from a Pyrobaculum aerophilum ribosomal protein. PaDBS1R6F10 exhibited anti-infective potential as it decreased the bacterial burden in murine Pseudomonas aeruginosa cutaneous infections by more than 1000-fold. Adverse cytotoxic and hemolytic effects were not detected against mammalian cells. The peptide demonstrated structural plasticity in terms of its secondary structure in the different environments tested. PaDBS1R6F10 represents a promising antimicrobial agent against bacteria infections, without harming human cells.

Published
2021

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