Crytic antimicrobial peptides hidden in protein precursors: identification of novel bioactive molecules

2017-04-08

Antibiotics are the mainstay in treatment of bacterial infections. However, resistance to antibacterial treatments has been rising since the 1970s, causing serious problems in the treatment and control of infectious diseases. Antibiotic resistance is now considered as one of the major global health threats of the 21st century in that the worldwide use of antibiotics is predicted to increase by more than 65% in the coming decades due to the increasing demand for meat and shift in agriculture practices in developing countries. New antibacterial drugs are urgently needed, but only three antibacterial drugs have been brought to the market since 1999 and very few new antibiotics are currently in development. This has prompted the search for alternatives to conventional antibiotics. Multiple alternative anti-infective strategies are being investigated, including vaccines, probiotics and phage therapy. Other promising alternatives to antibiotics are host defense peptides (HDPs), an important component of the first line of defense against infection, found in all multicellular organisms. HDPs are seen as true multifunctional peptides with activities as diverse as chemotaxis, inhibition of LPS-induced inflammation, modulation of leukocyte differentiation and promotion of wound healing. Interestingly, novel functions of these peptides are still being described to date. Many human proteins with functions not necessarily related to host defense behave as sources of HDPs. Some examples are lactoferrin, lysozyme and thrombin. Since these peptides are hidden in large proteins, they can be defined as “cryptic”. In order to identify by a rational approach further human proteins carrying cryptic HDPs, we recently developed an in-silico screening method to localize antimicrobial regions hidden inside the primary structure of precursor proteins. A wide list of potential new antimicrobial peptides was obtained by applying this method to about 4,000 human extracellular proteins. The main

Tesi di dottorato; NonPeerReviewed; info:eu-repo/semantics/doctoralThesis

Open access content. Open access content
info:eu-repo/semantics/openAccess

text
Italian
English

ITUDS oai:fedoa.unina.it:11638
Gaglione, Rosa (2017) Crytic antimicrobial peptides hidden in protein precursors: identification of novel bioactive molecules. [Tesi di dottorato]
10.6093/UNINA/FEDOA/11638
1357579405

UNIV DEGLI STUDI DI NAPOLI FEDERICO II
From OAIster®, provided by the OCLC Cooperative.

edsoai.on1357579405