Biomedical subjects

Y R Lo

Publications and source records attributed to Y R Lo.

3 recordsLinked to original sources

PubMed2001

Exploring the recognized bio-mimicry materials for gas sensing.

This study was undertaken to synthesize peptides that are partially similar to the binding sites of human olfactory receptor protein. First, a putative 3-D model structure of human olfactory receptor protein (P30953) was modeled using a molecular simulation method. The computer docking simulation was then performed to determine the most plausible binding sites between the model structure and target gases, trimethylamine, ammonia, acetic acid, and o-xylene. According to the simulation result, a series of polypeptide sequences, horp61 for TMA, horp103 for o-xylene, horp109 for ammonia, and horp193 for acetic acid as recognized molecules were designed for gas sensing purposes. Preparing these peptides as corresponding gas sensing probes, the results showed a high relative sensitivity response of 6.7 for TMA (probe horp61), 5.1 for o-xylene (probe horp103), 11 for ammonia (probe horp109), and 28 for acetic acid (probe horp193), respectively. These results indicate that peptide mimicking of binding domain on olfactory receptor opens a new window and offers a novel strategy for the further development of recognized materials for gas sensing.

Amino Acid Sequence↗

PubMed2000

Synthetic peptide mimicking of binding sites on olfactory receptor protein for use in 'electronic nose'.

A putative tertiary structure model of the dog's olfactory receptor (olfd canfa) is established in this study. By using a target odorous compound (trimethylamine), it is possible to locate the most plausible binding sites between the receptor model structure and the target odorous molecules through computer docking simulations. The two short oligo-peptide sequences (orp61 and orp188) for trimethylamine sensing were identified, synthesized, purified and coated onto the surface of the separate piezoelectric gold electrodes. These two peptides show a high binding capability for trimethylamine. To further enhance the sensitivity of the polypeptides towards the target compound, the polarity and the degree of docking were changed by a site-specific modification technique. The orp61 sequence was modified by substituting two amino acids in the binding pocket resulting in 33% increase in sensitivity towards trimethylamine and reduced noises from other non-target chemicals. The techniques used in the present study offer a unique approach for synthesizing peptides in mimicking binding domain of olfactory receptors. The approach can be easily applied to further development of recognized molecules for gas sensing, especially for use in 'electronic noses'.

Amino Acid Sequence↗

PubMed1998

Structural factors affect the interactions of anticardiotoxin antibodies and cobra venom cardiotoxins.

Two antibody preparations against cardiotoxins were raised by immunizing rabbits with cardiotoxin 1 and cardiotoxin 3, respectively. The two antibody preparations showed precipitin reactions with cardiotoxins 1, 2, 3 and 5, respectively. However, the results of competitive enzyme-linked immunoassay revealed that the respective cardiotoxin molecules exhibited different reactivity toward anticardiotoxin antibodies. Moreover, the order of reactivity with antibodies was not in line with the degree of their sequence identity. This suggest that the anticardiotoxin antibodies may recognize conformational epitopes rather than sequential ones in the toxin molecules. Alternatively, the four cardiotoxins reacted well with the antibodies in the absence of competitor, suggesting that sequence variations with cardiotoxin molecules may not exclusively influence the potential use of the anticardiotoxin antibodies for the neutralization of the activity of cardiotoxin variants.

Amino Acid Sequence↗