ANTIMIC: a database of antimicrobial sequences

Brahmachary, Manisha; Krishnan, S. P. T.; Koh, Judice L.Y.; Khan, Mohammad Asif; Seah, Seng Hong; Tan, Tin Wee; Brusic, Vladimir; Bajic, Vladimir B.

doi:10.1093/nar/gkh032

Cited by 132 publications

(85 citation statements)

References 24 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Antimicrobial peptides (AMPs) form the first line of defense against infection [6][7][8][9][10][11][12][13][14][15] and represent a new family of antibiotics that have been extensively studied. The AMPs described in the literature not only have antibacterial activities, but some also efficiently kill fungi, viruses and cancer cells [13][14][15].…”

Section: Introductionmentioning

confidence: 99%

See 1 more Smart Citation

The antifungal effect of peptides from hymenoptera venom and their analogs

et al. 2011

View full text Add to dashboard Cite

As the occurrence of Candida species infections increases, so does resistance against commonly-used antifungal agents. It is therefore necessary to look for new antifungal drugs. This study investigated the antifungal activity of recently isolated, synthesized and characterized antimicrobial α-helical amphipathic peptides (12–18 amino acids long) from the venom of hymenoptera (melectin, lasioglossins I, II, and III, halictines I and II) as well as a whole series of synthetic analogs. The minimal inhibitory concentrations (MICs) against different Candida species (C. albicans, C. krusei, C. glabrata, C. tropicalis and C. parapsilosis) of the natural peptides amounted to 4–20 µM (7–40 mg/l). The most active were the synthetic analog all-D-lasioglossin III and lasioglossin III analog KNWKK-Aib-LGK-Aib-IK-Aib-VK-NH2. As shown using a) colony forming unit determination on agar plates, b) the efflux of the dye from rhodamine 6B-loaded cells, c) propidium iodide and DAPI staining, and d) fluorescently labeled antimicrobial peptide (5(6)-carboxyfluorescein lasioglossin-III), the killing of fungi by the peptides studied occurs within minutes and might be accompanied by a disturbance of all membrane barriers. The peptides represent a promising lead for the development of new, effective antifungal drugs.

show abstract

Section: Introductionmentioning

confidence: 99%

“…The AMPs described in the literature not only have antibacterial activities, but some also efficiently kill fungi, viruses and cancer cells [13][14][15]. The significant advantage of AMPs lies in their mechanism of action, which is different from that of conventional antibiotics.…”

Section: Introductionmentioning

confidence: 99%

The antifungal effect of peptides from hymenoptera venom and their analogs

et al. 2011

View full text Add to dashboard Cite

show abstract

“…They have been identified in all kinds of species, including plants, insects, animals, and humans (13). The total number of known HDPs is increasing every year, with >900 HDPs listed in three databases to date (14)(15)(16).…”

Section: Introductionmentioning

confidence: 99%

Host Defense Peptides in Wound Healing

Steinstraesser

Koehler

Jacobsen

et al. 2008

Mol Med

143

112

View full text Add to dashboard Cite

Host defense peptides are effector molecules of the innate immune system. They show broad antimicrobial action against gram-positive and -negative bacteria, and they likely play a key role in activating and mediating the innate as well as adaptive immune response in infection and inflammation. These features make them of high interest for wound healing research. Nonhealing and infected wounds are a major problem in patient care and health care spending. Increasing infection rates, growing bacterial resistance to common antibiotics, and the lack of effective therapeutic options for the treatment of problematic wounds emphasize the need for new approaches in therapy and pathophysiologic understanding. This review focuses on the current knowledge of host defense peptides affecting wound healing and infection. We discuss the current data and highlight the potential future developments in this field of research.

show abstract

“…Gene encoded antimicrobial peptides (AMPs) are now well known to be a pervasive component of the immune defense system all across the plant and animal kingdom [14]. Hundreds of such peptides have been discovered from a plethora of living organisms, and many have been synthesized in laboratories with the aim of designing active molecules to combat antibiotic-resistant bacterial strains [2]. Indeed, our knowledge and comprehension of how AMPs function to kill microbial cells by nonspecific disruption of the plasma membrane lipid bilayer has improved significantly in recent years.…”

Section: Introductionmentioning

confidence: 99%

Molecular dynamics investigation of the influence of anionic and zwitterionic interfaces on antimicrobial peptides’ structure: Implications for peptide toxicity and activity

Khandelia

Kaznessis

2006

Peptides

View full text Add to dashboard Cite

Molecular dynamics simulations of three related helical antimicrobial peptides have been carried out in zwitterionic diphosphocholine (DPC) micelles and anionic sodiumdodecylsulfate (SDS) micelles. These systems can be considered as model mammalian and bacterial membrane interfaces, respectively. The goal of this study is to dissect the differences in peptide composition which make the mutant peptides (novispirin-G10 and novispirin-T7) less toxic than the parent peptide ovispirin (OVIS), although all three peptides have highly antibacterial properties. Compared to G10 and T7, OVIS inserts deepest into the DPC micelle. This correlates well with the lesser toxicity of G10 and T7. There is strong evidence which suggests that synergistic binding of hydrophobic residues drives binding of OVIS to the micelle. The helical content of G10 and T7 is reduced in the presence of DPC, and this leads to less amphipathic peptide structures, which bind weakly to the micelle. Simulations in SDS were carried out to compare the influence of membrane electrostatics on peptide structure. All three peptides bound strongly to SDS, and retained helical form. This corresponds well with their equally potent antibacterial properties. Based on the simulations, we argue that secondary structure stability often leads to toxic properties. We also propose that G10 and T7 operate by the carpet mechanism of cell lysis. Toxicity of peptides operating by the carpet mechanism can be attenuated by reducing the peptide helical content. The simulations successfully capture experimental binding states, and the different depths of binding of the three peptides to the two micelles correlate with their antibacterial and toxic properties.

show abstract

ANTIMIC: a database of antimicrobial sequences

Cited by 132 publications

References 24 publications

The antifungal effect of peptides from hymenoptera venom and their analogs

The antifungal effect of peptides from hymenoptera venom and their analogs

Host Defense Peptides in Wound Healing

Molecular dynamics investigation of the influence of anionic and zwitterionic interfaces on antimicrobial peptides’ structure: Implications for peptide toxicity and activity

Contact Info

Product

Resources

About