Results 111 to 120 of about 11,509 (217)

Melittin alcalase-hydrolysate: a novel chemically characterized multifunctional bioagent; antibacterial, anti-biofilm and anticancer

Frontiers in Microbiology
The prevalent life-threatening microbial and cancer diseases and lack of effective pharmaceutical therapies created the need for new molecules with antimicrobial and anticancer potential.
Samia E. El-Didamony, Mohamed H. Kalaba, Mohamed H. Sharaf, Esmail M. El-Fakharany, Esmail M. El-Fakharany, Esmail M. El-Fakharany, Ali Osman, Ali Osman, Ali Osman, Mahmoud Sitohy, Basel Sitohy, Basel Sitohy   +11 more
doaj   +1 more source

Effects of 1-butyl-3-methyl-imidazolium acetate on the solution behavior of melittin: A molecular dynamics study

Journal of Ionic Liquids
Ionic liquids posses efficiency as solvents, co-solvents or agents for applications involving biomolecules. Due to the increasing interest in systems containing proteins and ionic liquids, we hereby present results from molecular dynamics simulations on ...
Jessé Neumann, Hubert K. Stassen
doaj   +1 more source

Isolation of Melittin from Iranian Honey Bee Venom and Investigation of Its Effect on Proliferation of Cervical Cancer- HeLa Cell Line

Majallah-i Dānishgāh-i ’Ulūm-i Pizishkī-i Shahīd Ṣadūqī Yazd, 2013
Introduction: Cervical cancer is the second prevalent cancer in developing countries and the sixth prevalent cancer in USA. Since conventional treatment methods are associated with detrimental side effects, searching for new drugs using natural ...
K Pooshang Bagheri, A Mahmoodzadeh, H Zarinnahad, M Mahdavi, D Shahbazzadeh, A Moradi   +5 more
doaj  

Potential Inhibitory Effect of the Peptide Melittin Purified from Apis mellifera Venom on CTX-M-Type Extended-Spectrum β-Lactamases of Escherichia coli

Antibiotics
Background. Extended-spectrum β-lactamases (ESBLs) hydrolyze nearly all β-lactam antibiotics, affecting one of the most important groups of antimicrobials used in Gram-negative infections. Among them, CTX-M is the most widespread type of ESBL. This study
Sheril Ramos-Alcántara, María Alejandra Cornejo Napan, Giovanni Lopez Campana, Jesus Tamariz   +3 more
doaj   +1 more source

Effects of membrane channel-forming polypeptides on mitochondrial oxidative phosphorylation. A comparison of alamethicin, gramicidin A, melittin and tetraacetyl melittin

, 1985
Transmembrane channel-forming polypeptides can function as uncouplers of mitochondrial oxidative phosphorylation. The observed effects are dependent on the phosphate ion (Pi) concentration in the medium.
Balaram, P., Basu, A., Das, M. K.
core   +2 more sources

Interaction of Melittin Peptides with Perfluorocarbon Nanoemulsion Particles

, 2016
Melittin, an antimicrobial peptide, forms pores in biological membranes and triggers cell death. Therefore, it has potential as an anticancer therapy.
Paul H. Schlesinger (1318359), Nathan A. Baker (361291), Samuel A. Wickline (585136), Sun-Joo Lee (2132536), Gregory M. Lanza (132368)   +4 more
core   +1 more source

Discovery of Melittin as Triple-Action Agent: Broad-Spectrum Antibacterial, Anti-Biofilm, and Potential Anti-Quorum Sensing Activities

Molecules
The development of antibiotic-resistant microorganisms is a major global health concern. Recently, there has been an increasing interest in antimicrobial peptides as a therapeutic option.
Hongyan Yang, Rong Ma, Jiarou Chen, Qian Xie, Wenhui Luo, Pinghua Sun, Zheng Liu, Jialiang Guo   +7 more
doaj   +1 more source

Concentration-Dependent Modes of Melittin-Induced Membrane Destabilization: An Integration of Experimental and Computational Tools. [PDF]

Langmuir
Chacón Calderón A, Zelenovskii P, Soares M, Wrobel EC, Oliveira ON, Pereira D, Sardo M, Mafra L, Barros-Timmons A, Marín-Montesinos I.   +9 more
europepmc   +2 more sources

Cardiolipin-Specific Targeting of Melittin via Arg22 in Lipid Membranes: A Natural Toxin-Based Strategy for Treating Mitochondrial Dysfunction in Aging and Disease. [PDF]

Toxins (Basel)
Abaza SMSM, Zhou J, Wang Z, Pan Z, Ma H, Sun Y, Dagda RK, Gasanoff ES.   +7 more
europepmc   +1 more source

Comparative activities of cecropin A, melittin, and cecropin A-melittin peptide CA(1-7)M(2-9)NH2 against multidrug-resistant nosocomial isolates of Acinetobacter baumannii.

, 2003
The in vitro activity of three polycationic peptides, cecropin A, melittin, and cecropin A-melittin hybrid peptide CA(1-7)M(2-9)NH2, alone and in combination with various clinically used antimicrobial agents, was investigated against 32 nosocomial ...
CIRIONI, OSCAR, GIACOMETTI, Andrea, Kamysz W, Del Prete MS, SILVESTRI, Carmela, D'Amato G, SCALISE, Giorgio, Łukasiak J   +7 more
core