Mei Chiao Lin

Learn More
Amylin is a 37-amino acid cytotoxic constituent of amyloid deposits found in the islets of Langerhans of patients with type II diabetes. Extracellular accumulation of this peptide results in damage to insulin-producing beta cell membranes and cell death. We report here that at cytotoxic concentrations, amylin forms voltage-dependent, relatively(More)
Prions cause neurodegenerative disease in animals and humans. Recently it was shown that a 21-residue fragment of the prion protein (106-126) could be toxic to cultured neurons. We report here that this peptide forms ion-permeable channels in planar lipid bilayer membranes. These channels are freely permeable to common physiological ions, and their(More)
Alzheimer's disease (AD) pathology is characterized by plaques, tangles, and neuronal cell loss. The main constituent of plaques is beta-amyloid peptide (A beta), a 39-42 residue peptide which has been linked to disruption of calcium homeostasis and neurotoxicity in vitro. We demonstrate that a neurotoxic fragment of A beta, A beta (25-35) spontaneously(More)
Substantial genetic and biochemical evidence implicates amyloid peptides (Abeta) in the etiology of Alzheimer's Disease (AD). Recent evidence indicates that Abeta1-42 is the predominant species in the hallmark senile amyloid plaque of AD. Furthermore, Abeta1-42 forms aggregates inside lysosomes of cultured neurons leading to lysosomal disruption and cell(More)
Polyglycolide (PGA) and chitosan mixture solution was prepared using solvents of low toxicity to create novel, porous, biocompatible, degradable, and modifiable hybrid matrices for biomedical applications. The porosity of these PGA-chitosan hybrid matrices (P/C matrices) was created by a thermally induced phase separation method. Two types of the P/C hybrid(More)
Cell free extracts of Pseudomonas MS previously have been shown to carry out the synthesis of a novel amino acid, N-methylalanine (Kung, H.F., and Wagner, C. (1970) Biochim. Biophys. Acta 201, 513-516). An enzyme has been isolated from this organism which is responsible for the synthesis of N-methylalanine. The stoichiometry of the reaction catalyzed by(More)
Reduction of the protein-S-S-R bond in the zymogen of streptococcal proteinase leads to an enzymatically active molecule without any proteolysis being required. This conclusion is based upon experiments in which the zymogen has been reduced in very dilute solution where the rate of bimolecular autodigestion is at a minimum. Under these conditions, even in(More)
Several peptides contained within the amino acid sequence -Glu-Gly-Asn-Pro-Tyr-Val-Pro-Val-His-Phe-Asp-Ala-SerVal-OH at the carboxyl end of ribonuclease A were synthesized in which phenylalanine-120 was replaced by leucine, isoleucine, or tryptophan: [Leul*O]-RNase 111-124, [Ile120]RNase 111-124, [Trp’*Ol-RNase 111-124, ple*20]-RNase 113124, [Leul*O]-RNase(More)