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Right-Handed 14-Helix In Β3-Peptides From L-Aspartic Acid Monomers, Kamaljit Kaur, Tara Sprules, Wael Soliman, Reem Beleid, Sahar Ahmed Jan 2008

Right-Handed 14-Helix In Β3-Peptides From L-Aspartic Acid Monomers, Kamaljit Kaur, Tara Sprules, Wael Soliman, Reem Beleid, Sahar Ahmed

Pharmacy Faculty Articles and Research

β-Peptides made from L-aspartic acid monomers form a new class of β3-peptides. Here we report the first three-dimensional NMR solution structure of a β3-hexapeptide (1) from L-aspartic acid monomers in 2,2,2-trifluoroethanol (TFE). We show that 1 forms a right-handed 14-helical structure in TFE. α-peptides from naturally occurring L-amino acids adopt a right-handed α-helix whereas β3-peptides formed from β3-amino acids derived from naturally occurring L-amino acids form left-handed 14-helices. The right-handed 14-helical conformation of 1 is a better mimic of α-peptide conformations. Using the NMR structure of 1 in TFE, we …


Enzymatic Processing Of Amelogenin During Continuous Crystallization Of Apatite, Vuk Uskoković, M.-K. Kim, W. Li, S. Habelitz Jan 2008

Enzymatic Processing Of Amelogenin During Continuous Crystallization Of Apatite, Vuk Uskoković, M.-K. Kim, W. Li, S. Habelitz

Pharmacy Faculty Articles and Research

Dental enamel forms through a protein-controlled mineralization and enzymatic degradation with a nanoscale precision that new engineering technologies may be able to mimic. Recombinant fulllength human amelogenin (rH174) and a matrix-metalloprotease (MMP-20) were employed in a pHstat titration system that enabled a continuous supply of calcium and phosphate ions over several days, mimicking the initial stages of matrix processing and crystallization in enamel in-vitro. Effects on the self-assembly and crystal growth from a saturated aqueous solution containing 0.4 mg/ml rH174 and MMP-20 with the weight ratio of 1:1000 with respect to rH174 were investigated. A transition from nanospheres to fibrous …


Discordance In The Paraoxonase (Pon1)-192qr Polymorphism, Rozaida @ Poh Yuen Ying Dec 2007

Discordance In The Paraoxonase (Pon1)-192qr Polymorphism, Rozaida @ Poh Yuen Ying

Rozaida @ Poh Yuen Ying

Paraoxonase (PON1) has been implicated to have a cardioprotective role, due to its physical attachment with high-density lipoprotein. PON1192QR is a variation of the PON1 gene, the R allele being a risk factor for cardiovascular disease. Kinetic studies resulting in a plot of paraoxon versus diazoxon hydrolysis rates may be used to accurately predict PON1192 geno-type. In this study, paraoxonase and diazoxonase activities in plasma were measured spec-trophotometrically using plasma while PCR-based PON1192 genotyping was performed us-ing polymerase chain reaction followed by restriction digestion. The two-substrate assay-derived genotypes were cross-referred with those determined by PCR-based genotyping. When results did not …