Intramolecular Modulation of Serine Protease Inhibitor Activity in a Marine Cyanobacterium with Antifeedant Properties

Extracts of the Floridian marine cyanobacterium Lyngbya cf. confervoides were found to deter feeding by reef fish and sea urchins (Diadema antillarum). This antifeedant activity may be a reflection of the secondary metabolite content, known to be comprised of many serine protease inhibitors. Further...
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Autor*in:	Susan Matthew [verfasserIn] Ranjala Ratnayake [verfasserIn] Mikel A. Becerro [verfasserIn] Raphael Ritson-Williams [verfasserIn] Valerie J. Paul [verfasserIn] Hendrik Luesch [verfasserIn]

Format:	E-Artikel
Sprache:	Englisch

Erschienen:	2010

Schlagwörter:	cyanobacteria;Lyngbya antifeedant activity serine protease inhibitors cyclodepsipeptides

Übergeordnetes Werk:	In: Marine Drugs - MDPI AG, 2005, 8(2010), 6, Seite 1803-1816
Übergeordnetes Werk:	volume:8 ; year:2010 ; number:6 ; pages:1803-1816

Links:	Link aufrufen Link aufrufen Link aufrufen Journal toc

DOI / URN:	10.3390/md8061803

Katalog-ID:	DOAJ085360570

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language	English
source	In Marine Drugs 8(2010), 6, Seite 1803-1816 volume:8 year:2010 number:6 pages:1803-1816
sourceStr	In Marine Drugs 8(2010), 6, Seite 1803-1816 volume:8 year:2010 number:6 pages:1803-1816
format_phy_str_mv	Article
institution	findex.gbv.de
topic_facet	cyanobacteria;Lyngbya antifeedant activity serine protease inhibitors cyclodepsipeptides Biology (General)
isfreeaccess_bool	true
container_title	Marine Drugs
authorswithroles_txt_mv	Susan Matthew @@aut@@ Ranjala Ratnayake @@aut@@ Mikel A. Becerro @@aut@@ Raphael Ritson-Williams @@aut@@ Valerie J. Paul @@aut@@ Hendrik Luesch @@aut@@
publishDateDaySort_date	2010-01-01T00:00:00Z
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callnumber-first	Q - Science
author	Susan Matthew
spellingShingle	Susan Matthew misc QH301-705.5 misc cyanobacteria;Lyngbya misc antifeedant activity misc serine protease inhibitors misc cyclodepsipeptides misc Biology (General) Intramolecular Modulation of Serine Protease Inhibitor Activity in a Marine Cyanobacterium with Antifeedant Properties
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topic_title	QH301-705.5 Intramolecular Modulation of Serine Protease Inhibitor Activity in a Marine Cyanobacterium with Antifeedant Properties cyanobacteria;Lyngbya antifeedant activity serine protease inhibitors cyclodepsipeptides
topic	misc QH301-705.5 misc cyanobacteria;Lyngbya misc antifeedant activity misc serine protease inhibitors misc cyclodepsipeptides misc Biology (General)
topic_unstemmed	misc QH301-705.5 misc cyanobacteria;Lyngbya misc antifeedant activity misc serine protease inhibitors misc cyclodepsipeptides misc Biology (General)
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title	Intramolecular Modulation of Serine Protease Inhibitor Activity in a Marine Cyanobacterium with Antifeedant Properties
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title_full	Intramolecular Modulation of Serine Protease Inhibitor Activity in a Marine Cyanobacterium with Antifeedant Properties
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title_sort	intramolecular modulation of serine protease inhibitor activity in a marine cyanobacterium with antifeedant properties
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title_auth	Intramolecular Modulation of Serine Protease Inhibitor Activity in a Marine Cyanobacterium with Antifeedant Properties
abstract	Extracts of the Floridian marine cyanobacterium Lyngbya cf. confervoides were found to deter feeding by reef fish and sea urchins (Diadema antillarum). This antifeedant activity may be a reflection of the secondary metabolite content, known to be comprised of many serine protease inhibitors. Further chemical and NMR spectroscopic investigation led us to isolate and structurally characterize a new serine protease inhibitor 1 that is formally derived from an intramolecular condensation of largamide D (2). The cyclization resulted in diminished activity, but to different extents against two serine proteases tested. This finding suggests that cyanobacteria can endogenously modulate the activity of their protease inhibitors.
abstractGer	Extracts of the Floridian marine cyanobacterium Lyngbya cf. confervoides were found to deter feeding by reef fish and sea urchins (Diadema antillarum). This antifeedant activity may be a reflection of the secondary metabolite content, known to be comprised of many serine protease inhibitors. Further chemical and NMR spectroscopic investigation led us to isolate and structurally characterize a new serine protease inhibitor 1 that is formally derived from an intramolecular condensation of largamide D (2). The cyclization resulted in diminished activity, but to different extents against two serine proteases tested. This finding suggests that cyanobacteria can endogenously modulate the activity of their protease inhibitors.
abstract_unstemmed	Extracts of the Floridian marine cyanobacterium Lyngbya cf. confervoides were found to deter feeding by reef fish and sea urchins (Diadema antillarum). This antifeedant activity may be a reflection of the secondary metabolite content, known to be comprised of many serine protease inhibitors. Further chemical and NMR spectroscopic investigation led us to isolate and structurally characterize a new serine protease inhibitor 1 that is formally derived from an intramolecular condensation of largamide D (2). The cyclization resulted in diminished activity, but to different extents against two serine proteases tested. This finding suggests that cyanobacteria can endogenously modulate the activity of their protease inhibitors.
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title_short	Intramolecular Modulation of Serine Protease Inhibitor Activity in a Marine Cyanobacterium with Antifeedant Properties
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Intramolecular Modulation of Serine Protease Inhibitor Activity in a Marine Cyanobacterium with Antifeedant Properties

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