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Intramolecular modulation of serine protease inhibitor activity in a marine cyanobacterium with antifeedant properties.

Matthew S, Ratnayake R, Becerro MA, Ritson-Williams R, Paul VJ, Luesch H - Mar Drugs (2010)

Bottom Line: Extracts of the Floridian marine cyanobacterium Lyngbya cf. confervoides were found to deter feeding by reef fish and sea urchins (Diadema antillarum).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.

View Article: PubMed Central - PubMed

Affiliation: Department of Medicinal Chemistry, University of Florida, Gainesville, FL 32610, USA. susmatt@ufl.edu

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.

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Effect of compounds 1 and 2 on chymotrypsin and elastase activity.
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f5-marinedrugs-08-01803: Effect of compounds 1 and 2 on chymotrypsin and elastase activity.

Mentions: The presence of an Ahp unit is characteristic for many serine protease inhibitors, including lyngbyastatins. Largamide D (2) was previously reported to be a moderate chymotrypsin inhibitor [24]. We directly compared the activities of compound 1 and largamide D (2) against two serine proteases, chymotrypsin and porcine pancreatic elastase (Figure 5, Table 2). Compound 1 exhibited 11-fold and 33-fold reduced activity against chymotrypsin and elastase, respectively, indicating that the condensation of Ahp and Thr-1 considerably deactivated largamide D (2) and to different extents for both enzymes tested.


Intramolecular modulation of serine protease inhibitor activity in a marine cyanobacterium with antifeedant properties.

Matthew S, Ratnayake R, Becerro MA, Ritson-Williams R, Paul VJ, Luesch H - Mar Drugs (2010)

Effect of compounds 1 and 2 on chymotrypsin and elastase activity.
© Copyright Policy - open-access
Related In: Results  -  Collection

License 1 - License 2
Show All Figures
getmorefigures.php?uid=PMC2901826&req=5

f5-marinedrugs-08-01803: Effect of compounds 1 and 2 on chymotrypsin and elastase activity.
Mentions: The presence of an Ahp unit is characteristic for many serine protease inhibitors, including lyngbyastatins. Largamide D (2) was previously reported to be a moderate chymotrypsin inhibitor [24]. We directly compared the activities of compound 1 and largamide D (2) against two serine proteases, chymotrypsin and porcine pancreatic elastase (Figure 5, Table 2). Compound 1 exhibited 11-fold and 33-fold reduced activity against chymotrypsin and elastase, respectively, indicating that the condensation of Ahp and Thr-1 considerably deactivated largamide D (2) and to different extents for both enzymes tested.

Bottom Line: Extracts of the Floridian marine cyanobacterium Lyngbya cf. confervoides were found to deter feeding by reef fish and sea urchins (Diadema antillarum).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.

View Article: PubMed Central - PubMed

Affiliation: Department of Medicinal Chemistry, University of Florida, Gainesville, FL 32610, USA. susmatt@ufl.edu

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.

Show MeSH
Related in: MedlinePlus