Linked Life Data

18403141

Source:http://linkedlifedata.com/resource/pubmed/id/18403141

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1-2
pubmed:dateCreated
2008-4-29
pubmed:abstractText
Carboxymethyl high amylose starch (CM-HAS) and succinate high amylose starch (S-HAS) were proposed as pharmaceutical excipients for oral drug delivery, providing a significant gastroprotection to dosage forms of pancreatic enzymes (alpha-amylase, lipase and trypsin) compared to unprotected enzymes. In acidic medium, carboxylic groups are protonated (at least in tablet surface) ensuring local buffering properties and giving a compact shape of the tablets. The enzymes were formulated individually or in association as three enzymes formulation. After the first hour of incubation (over a 2h experiment) in simulated gastric fluid (SGF), the three pancreatic enzymes retained an overall (average of the three enzymes) activity of 72% when formulated as tablets with CM-HAS excipient and 77% when formulated with S-HAS excipient. Furthermore, after incubation in SGF, the delivery of 75% of the total remaining enzymatic activity in the simulated intestinal fluid (SIF) taken 180 and 170 min for CM-HAS and S-HAS, respectively. Both formulations with carboxylated starch as excipient have a high loading capacity (up to 70-80% enzymes), which is of interest for pancreatic enzymes replacement therapy of pancreatitis. An advantage of these formulations is that gastroprotection is afforded by the carboxylated matrices (carboxylic groups), without enteric coating.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0378-5173
pubmed:author
pubmed:issnType
Print
pubmed:day
22
pubmed:volume
356
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
212-23
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
2008
pubmed:articleTitle
Carboxylated high amylose starch as pharmaceutical excipients. Structural insights and formulation of pancreatic enzymes.
pubmed:affiliation
Department of Chemistry and Centre BioMed, Université du Québec à Montréal, CP 8888, Succursale A, Montreal, Quebec H3C 3P8 Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't