Biomedical Engineering Reference
In-Depth Information
Table 3.1  Biological activities reported for lasso peptides
Name
Producer
Class a
Biological activities References
Lasso peptides from actinobacteria
Siamycin
I/ MS-271/
NP-06
Streptomyces sp.
I
Anti-HIV
Antibacterial
Inhibitor of myosin
light chain kinase
(Chokekijchai et al. 1995 ;
Detlefsen et al. 1995 ;
Tsunakawa et al.
1995 ; Lin et al. 1996 ;
Yano et al. 1996 )
Siamycin II
Streptomyces sp.
I
Anti-HIV
Antibacterial
(Constantine et al. 1995 ;
Tsunakawa et al.
1995 )
RP 71955/
Aborycin
Streptomyces sp.
I
Anti-HIV
Antibacterial
(Helynck et al. 1993 ; Pot-
terat et al. 1994 )
Sviceucin/
SSV-2083
Streptomyces sviceus
I
Antibacterial
(Ducasse et al. 2012a )
Anantin
Streptomyces
coerulescens
II
Atrial natriuretic
factor antagonist
(Weber et al. 1991 )
Propeptin
Microbispora sp.
II
Prolyloligopeptidase
inhibitor
Weakly antibacterial
(Kimura et al. 1997a )
Lariatin
Rhodococcus jostii
II
Antimycobacterial
(Iwatsuki et al. 2006 )
Sungsanpin
Streptomyces sp.
II
Inhibitory activity
in a cell invasion
assay with a lung
cancer cell line
(Um et al. 2013 )
BI-32169
III
Glucagon receptor
antagonist
(Potterat et al. 2004 ;
Knappe et al. 2010 )
Lasso peptides from proteobacteria
RES-701-1
RES-701-3
Streptomyces sp.
II
Endothelin type
B receptor
antagonist
(Tanaka et al. 1994 ;
Ogawa et al. 1995 )
Microcin J25
(MccJ25)
Escherichia coli
II
Antibacterial
RNA polymerase 
inhibition
(Salomón and Farías
1992 ; Bayro et al.
2003 ; Rosengren et al. 
2003 ; Wilson et al.
2003 )
Capistruin
Burkholderia
thailandensis
II
Antibacterial
RNA polymerase 
inhibition
(Knappe et al. 2008 ;
Knappe et al. 2009 )
Astexin-1
Asticcacaulis
excentricus
II
Antibacterial
(Maksimov et al. 2012 )
a The classification refers to the number of disulfide bridges that further stabilize the lasso struc-
ture and has been described in Chap. 2. Classes I, II and III are characterized by two, zero and one
disulfide bridge(s), respectively
ET A and ET B . The ET A and ET B  receptors are G protein-coupled receptors (GPCRs) 
with seven transmembrane domains. The ET A receptor binds ET-1 and ET-2 with
an affinity two orders of magnitude higher than that for ET-3 (  K i ~ 0.01-0.1 and
1-3 nM, respectively), while the ET B receptor binds all three isoforms with similar
affinity (  K i ~ 0.01-0.02 nM; Williams et al. 1991 ; Schiffrin 2001 ). In blood vessels,
 
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