Antimicrobial Peptides Discovery, Design and Novel Therapeutic Strategies
The book commences with a vivid and inspiring introduction contributed by Professor Michael Zasloff, a distinguished forerunner in the field. Part I provides an overview of nomenclature, classifi cation and bioinformatic analysis of antimicrobial peptides from bacteria, plants and animals. Sub...
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CABI
2014
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oai:scholar.dlu.edu.vn:DLU123456789-369792023-11-11T05:27:20Z Antimicrobial Peptides Discovery, Design and Novel Therapeutic Strategies Guangshun, Guangshun Antimicrobial Therapeutic The book commences with a vivid and inspiring introduction contributed by Professor Michael Zasloff, a distinguished forerunner in the field. Part I provides an overview of nomenclature, classifi cation and bioinformatic analysis of antimicrobial peptides from bacteria, plants and animals. Subsequently, lantibiotics from bacteria and cyclotides from plants are presented. These unique peptide templates with multiple sulfur-mediated bridges are resistant to proteases, rendering them attractive for engineering new compounds for food preservation, pest control and curing diseases. Part II discusses database-aided peptide prediction and design methods, synthetic combinatorial libraries and peptide mimetics that expand the conformational space of natural antimicrobial peptides. These approaches also allow for the optimization of the desired properties and therapeutic index of the peptide analogues or mimicries. An in-depth understanding of the mode of action of these peptides is essential for drug development. As a consequence, Part III covers the biophysical and structural characterization of antimicrobial peptides and their complexes. While many peptides (e.g. magainin and protegrin-1) target bacterial membranes, apidaecin, buforin II, PR-39 and others can cross bacterial membranes and associate with internal targets such as heat-shock proteins and nucleic acids. Structural determination sheds light on how such peptides recognize membrane or non-membrane targets at atomic resolution, and provides the basis for structurebased peptide design. Finally, Part IV focuses on novel strategies for developing peptide-based therapies. These include liberating LL-37 from the inactive bound state in infected lungs, enhancing the expression of human cathelicidin and human β-defensin-2 by vitamin D, and stimulating immune responses to bacterial invasion by applying peptide analogues that may or may not kill bacteria directly. 2014-04-17T08:38:01Z 2014-04-17T08:38:01Z 2010 Book 978 1 84593 657 0 https://scholar.dlu.edu.vn/thuvienso/handle/DLU123456789/36979 en application/pdf CABI |
| institution |
Thư viện Trường Đại học Đà Lạt |
| collection |
Thư viện số |
| language |
English |
| topic |
Antimicrobial Therapeutic |
| spellingShingle |
Antimicrobial Therapeutic Guangshun, Guangshun Antimicrobial Peptides Discovery, Design and Novel Therapeutic Strategies |
| description |
The book commences with a vivid and inspiring introduction contributed by Professor
Michael Zasloff, a distinguished forerunner in the field. Part I provides an overview of
nomenclature, classifi cation and bioinformatic analysis of antimicrobial peptides from bacteria,
plants and animals. Subsequently, lantibiotics from bacteria and cyclotides from plants are
presented. These unique peptide templates with multiple sulfur-mediated bridges are resistant
to proteases, rendering them attractive for engineering new compounds for food preservation,
pest control and curing diseases. Part II discusses database-aided peptide prediction and
design methods, synthetic combinatorial libraries and peptide mimetics that expand the
conformational space of natural antimicrobial peptides. These approaches also allow for the
optimization of the desired properties and therapeutic index of the peptide analogues or
mimicries. An in-depth understanding of the mode of action of these peptides is essential for
drug development. As a consequence, Part III covers the biophysical and structural
characterization of antimicrobial peptides and their complexes. While many peptides (e.g.
magainin and protegrin-1) target bacterial membranes, apidaecin, buforin II, PR-39 and others
can cross bacterial membranes and associate with internal targets such as heat-shock proteins
and nucleic acids. Structural determination sheds light on how such peptides recognize
membrane or non-membrane targets at atomic resolution, and provides the basis for structurebased peptide design. Finally, Part IV focuses on novel strategies for developing peptide-based
therapies. These include liberating LL-37 from the inactive bound state in infected lungs,
enhancing the expression of human cathelicidin and human β-defensin-2 by vitamin D, and
stimulating immune responses to bacterial invasion by applying peptide analogues that may
or may not kill bacteria directly. |
| format |
Book |
| author |
Guangshun, Guangshun |
| author_facet |
Guangshun, Guangshun |
| author_sort |
Guangshun, Guangshun |
| title |
Antimicrobial Peptides
Discovery, Design and Novel Therapeutic
Strategies |
| title_short |
Antimicrobial Peptides
Discovery, Design and Novel Therapeutic
Strategies |
| title_full |
Antimicrobial Peptides
Discovery, Design and Novel Therapeutic
Strategies |
| title_fullStr |
Antimicrobial Peptides
Discovery, Design and Novel Therapeutic
Strategies |
| title_full_unstemmed |
Antimicrobial Peptides
Discovery, Design and Novel Therapeutic
Strategies |
| title_sort |
antimicrobial peptides
discovery, design and novel therapeutic
strategies |
| publisher |
CABI |
| publishDate |
2014 |
| url |
https://scholar.dlu.edu.vn/thuvienso/handle/DLU123456789/36979 |
| _version_ |
1782541734557777920 |