The synthesis of potential pharmacological chaperones and fluorogenic substrates for MPS I, IIIA and VII

2021 ◽  
Author(s):  
◽  
Gareth Doherty
Keyword(s):  
Fluorogenic Substrates ◽  
Pharmacological Chaperones ◽  
Mps I

Ultrasensitive Fluorogenic Substrates for Serine Proteases

1997 ◽  
Vol 78 (04) ◽  
pp. 1193-1201 ◽  
Author(s):  
Saulius Butenas ◽  
Maria E DiLorenzo ◽  
Kenneth G Mann
Keyword(s):  
Serine Proteases ◽  
Factor Viia ◽  
Activated Protein C ◽  
Factor Xa ◽  
High Specificity ◽  
High Rate ◽  
Fluorogenic Substrates ◽  
Type Plasminogen Activator ◽  
Factor Xia ◽  
Coagulation And Fibrinolysis

SummarySelective, sensitive assays for the quantitation of serine proteases involved in coagulation and fibrinolysis have been developed employing fluorogenic substrates containing a 6-amino-1-naphthalenesulfonamide leaving group (PNS-substrates). Over one hundred substrates were evaluated for hydrolysis by the serine proteases of blood coagulation and fibrinolysis, and substrate structure-efficiency correlations were examined. PNS-substrates which contain Lys in the P1 position are specific for Lys-plasmin and are either not hydrolyzed or hydrolyzed at a relatively low rate by factor Xa, thrombin, or urokinase-type plasminogen activator (uPA). These substrates allow quantitation of Lys-plasmin at concentrations as low as 1 pM. Eighteen of over 90 substrates tested for factor XIa are hydrolyzed by this enzyme at a relatively high rate reaching a kcat value of 170 s-1 and allowing quantitation of factor XIa at 10 fM. Eighteen of almost 90 PNS-substrates tested display high specificity for thrombin, some exceeding that for factor Xa by > 10,000-fold and > 100-fold for activated protein C (APC). Seven of these substrates have a over 100 s-1 and three of them have a KM below 1 μM. They allow the quantitation of thrombin at concentrations as low as 20 fM. For APC, uPA and the factor Vila/tissue factor complex, quantitation is feasible at 1 pM concentration. For factor Xa and factor VIIa the limits are 0.4 pM and 40 pM respectively. The PNS-substrates presented in this study may be employed for the development of direct and sensitive serine protease assays.

scholarly journals Sexual behaviour in a murine model of mucopolysaccharidosis type I (MPS I)

PLoS ONE ◽  
2019 ◽  
Vol 14 (12) ◽  
pp. e0220429 ◽  
Author(s):  
Ana Barbosa Mendes ◽  
Cinthia Castro do Nascimento ◽  
Vânia D’Almeida
Keyword(s):  
Sexual Behaviour ◽  
Murine Model ◽  
Type I ◽  
Mucopolysaccharidosis Type ◽  
Mucopolysaccharidosis Type I ◽  
Mps I

scholarly journals Neonatal tolerance induction enables accurate evaluation of gene therapy for MPS I in a canine model

2016 ◽  
Vol 119 (1-2) ◽  
pp. 124-130 ◽  
Author(s):  
Christian Hinderer ◽  
Peter Bell ◽  
Jean-Pierre Louboutin ◽  
Nathan Katz ◽  
Yanqing Zhu ◽  
...  
Keyword(s):  
Gene Therapy ◽  
Tolerance Induction ◽  
Canine Model ◽  
Accurate Evaluation ◽  
Mps I

New fluorogenic substrates for renin

1981 ◽  
Vol 110 (1) ◽  
pp. 232-239 ◽  
Author(s):  
Kazuo Murakami ◽  
Tamiko Ohsawa ◽  
Shigehisa Hirose ◽  
Katsumi Takada ◽  
Shumpei Sakakibara
Keyword(s):  
Fluorogenic Substrates

scholarly journals Glycomimetic-based pharmacological chaperones for lysosomal storage disorders: lessons from Gaucher, GM1-gangliosidosis and Fabry diseases

2016 ◽  
Vol 52 (32) ◽  
pp. 5497-5515 ◽  
Author(s):  
Elena M. Sánchez-Fernández ◽  
José M. García Fernández ◽  
Carmen Ortiz Mellet
Keyword(s):  
Lysosomal Storage Disorders ◽  
Lysosomal Storage ◽  
Future Outlook ◽  
Gm1 Gangliosidosis ◽  
Pharmacological Chaperones ◽  
Storage Disorders

Recent advancements and future outlook on pharmacological chaperones for lysosomal storage disorders using glycomimetics are discussed.

scholarly journals The natural history of MPS I: global perspectives from the MPS I Registry

2014 ◽  
Vol 16 (10) ◽  
pp. 759-765 ◽  
Author(s):  
Michael Beck ◽  
Pamela Arn ◽  
Roberto Giugliani ◽  
Joseph Muenzer ◽  
Torayuki Okuyama ◽  
...  
Keyword(s):  
Natural History ◽  
Global Perspectives ◽  
History Of ◽  
Mps I

Selective Neurotensin-Derived Internally Quenched Fluorogenic Substrates for Neurolysin (EC 3.4.24.16): Comparison with Thimet Oligopeptidase (EC 3.4.24.15) and Neprilysin (EC 3.4.24.11)

2001 ◽  
Vol 292 (2) ◽  
pp. 257-265 ◽  
Author(s):  
Vitor Oliveira ◽  
Marcelo Campos ◽  
Jefferson P. Hemerly ◽  
Emer S. Ferro ◽  
Antonio C.M. Camargo ◽  
...  
Keyword(s):  
Fluorogenic Substrates ◽  
Thimet Oligopeptidase

An alternative approach for the synthesis of fluorogenic substrates of endo-β-(1→4)-xylanases and some applications

2008 ◽  
Vol 343 (3) ◽  
pp. 541-548 ◽  
Author(s):  
Mária Vršanská ◽  
Wim Nerinckx ◽  
Marc Claeyssens ◽  
Peter Biely
Keyword(s):  
Fluorogenic Substrates ◽  
Alternative Approach
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