STICKINESS TO HYDROPHOBIC SURFACES VARIES WIDELY AMONG PEPTIDES AND PROTEINS

Abstract

To determine whether there are differences in stickiness to hydrophobic surfaces among peptides and proteins under immunoassay conditions, peptides and proteins were radio-labeled with ¹²⁵I and competitive adsorption with human serum albumin (HSA) in polystyrene or polypropylene tubes was used to determine the IC ₅₀, the concentration of HSA required to reduce the adsorption of the labeled polypeptides to 50% of maximal. Stickiness was defined as log₁₀(10⁹ I C ₅₀). Stickiness varied significantly between the labeled polypeptides (p < 0.00001) and ranged (±sem) from 0.99 ± 0.07 for angiotensin II to 5.30 ± 0.07 for tyr⁰-urocortin II. The stickiness of HSA and γ globulin was 1.62 ± 0.09 and 1.92 ± 0.05, respectively. No significant difference in stickiness between polystyrene and polypropylene was found. We conclude that some peptides are sufficiently sticky to risk adsorptive loss during sampling and analysis, and there may exist peptides so sticky that they remain uncharacterized.

Keywords:

• adsorption
• hydrophobic
• peptide
• protein
• stickiness
• surface

ACKNOWLEDGMENTS

We would like to thank the Canterbury District Health Board and the Canterbury Medical Research Foundation (CMRF) for supporting this work. The assistance of master's student Murray Whittaker and CMRF Summer Students Brian Ko, Mary Warren, and Emma Andrews is greatly appreciated, as is the technical assistance of Laurie Manley.