scholarly journals Low Molecular Weight Opioid Peptide Esters Could be Developed as a New Class of Analgesics

2011 ◽  
Vol 5 ◽  
pp. PMC.S6803 ◽  
Author(s):  
Joel S. Goldberg
Keyword(s):  
Molecular Weight ◽  
Chronic Pain ◽  
Opioid Peptide ◽  
Good Manufacturing Practice ◽  
Low Molecular Weight ◽  
Clinical Use ◽  
Plasma Stability ◽  
New Class ◽  
Animal Data ◽  
Peptide Esters

Low molecular weight opioid peptide esters (OPE) could become a class of analgesics with different side effect profiles than current opiates. OPE may have sufficient plasma stability to cross the blood brain barrier (BBB), undergo ester hydrolysis and produce analgesia. OPE of dipeptides, tyr-pro and tyr-gly conjugated to ethanol have a structure similar to the anesthestic agent, etomidate. Based upon the analgesic activity of dipeptide opioids, Lipinski's criteria, and permeability of select GABA esters to cross the BBB, opioid peptides (OP) conjugated to ethanol, cholesterol or 3-glucose are lead recommendations. Preliminary animal data suggests that tyr-pro-ethyl ester crosses the BBB and unexpectedly produces hyperalgesia. Currently, there are no approved OP analgesics available for clinical use. Clinical trials of good manufacturing practice OP administered to patients suffering from chronic pain with indwelling intrathecal pumps could resolve the issue that OP may be superior to opiates and may redirect research.

A New Class of Selective Low-Molecular-Weight Gelators Based on Salts of Diaminotriazinecarboxylic Acids

2006 ◽  
Vol 18 (16) ◽  
pp. 3616-3626 ◽  
Author(s):  
Olivier Lebel ◽  
Marie-Ève Perron ◽  
Thierry Maris ◽  
Sylvia F. Zalzal ◽  
Antonio Nanci ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Low Molecular Weight ◽  
New Class ◽  
Low Molecular Weight Gelators

Physicochemical properties of low molecular weight alkylated chitosans: A new class of potential nonviral vectors for gene delivery

2006 ◽  
Vol 51 (2) ◽  
pp. 140-148 ◽  
Author(s):  
Sebnem Ercelen ◽  
Xin Zhang ◽  
Guy Duportail ◽  
Christian Grandfils ◽  
Jacques Desbrières ◽  
...  
Keyword(s):  
Molecular Weight ◽  
Gene Delivery ◽  
Physicochemical Properties ◽  
Low Molecular Weight ◽  
Nonviral Vectors ◽  
New Class

scholarly journals Isolation and analysis of a non-protein low molecular weight thiol-mercurial adduct from human prostate lymph node cells (LNCaP)

2020 ◽  
Vol 40 (6) ◽  
Author(s):  
Michael Gronow
Keyword(s):  
Molecular Weight ◽  
Low Molecular Weight ◽  
Anion Exchange Column ◽  
Thiol Compounds ◽  
New Class ◽  
Prostate Cells ◽  
Intermediate Fraction ◽  
Lymph Node Cells ◽  
Protein Matrices ◽  
Malignant Prostate

Abstract Thiol compounds present in human malignant prostate cells (LNCaP) were investigated after reaction with a mercurial blocking reagent. After extracting the cellular glutathione and some other low molecular weight (LMW) thiols using trichloroacetic acid the resulting the protein precipitate was extracted with buffered 8 M urea containing 2-chloromercuri-4-nitrophenol in an equimolar amount to that of the thiol present. After removing the insoluble chromatin fraction the urea soluble labeled adducts formed were chromatographed on G15 Sephadex. Three yellow coloured (A410 nm) fractions were obtained; first, the excluded protein fraction containing 16.0 ± 4.1% of the applied label followed by an intermediate fraction containing 5.9 ± 1.2%. Finally a LMW fraction emerged which contained 77.2 ± 3.7% of the total label applied and this was further analyzed by column chromatography, first on an anion exchange column and then on a PhenylSepharose 6 column to give what appeared to be a single component. LC–MS analysis of this component gave a pattern of mercuri-clusters, formed on MS ionization showing possible parent ions at 704 or 588 m/z, the former indicating that a thiol fragment of molecular weight approximately 467 could be present. No fragments with a single sulfur adduct (a 369 m/z fragment) were observed The adduct was analyzed for cysteine and other amino acids, nucleic acid bases, ribose and deoxyribose sugars, selenium and phosphorus; all were negative leading to the conclusion that a new class of unknown LMW thiol is present concealed in the protein matrices of these cells.

Some Effects of Low Molecular Weight Dextran on Coagulation

1966 ◽  
Vol 15 (01/02) ◽  
pp. 118-130 ◽  
Author(s):  
Marion Dugdale ◽  
J.D Nofzinger ◽  
F Murphey
Keyword(s):  
Molecular Weight ◽  
Protective Action ◽  
Fibrin Clot ◽  
Low Molecular Weight ◽  
Clinical Use ◽  
Excessive Bleeding

SummaryLMDX has been shown to affect adversely the rate of prothrombin consumption during coagulation and the structure of the fibrin clot when present in the concentrations usually recommended for clinical use. Its use in animals with hemostatic defects induced by the pump-oxygenator was accompanied by excessive bleeding. At the same time, however, it conferred some form of protection which led to improved survival. A manner of using LMDX so as to benefit from its protective action without endangering hemostasis is currently under study.

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