Quantitative determination of the peptide retention of polymeric substrates using matrix-assisted laser desorption/ionization mass spectrometry.
Polymer surface-peptide binding interactions have been shown previously to lead to reductions in peptide matrix assisted laser desorption/ionization (MALDI) ion signals. In previous studies, increases in surface-peptide binding were characterized by the increases in both the initially adsorbed and retained quantities of 125I-radiolabeled peptides. The present studies establish a specific correlation between the peptide retention properties of the polymer surface and the reduction in the peptide MALDI ion signal. This correlation is demonstrated by obtaining MALDI mass spectra of angiotensin I applied to various polymer surfaces having a range of peptide adsorption and retention properties. In addition, the use of a MALDI based method of standard additions is shown to allow the quantitation of the polymer surface-peptide retention affinity for angiotensin I and porcine insulin. The MALDI standard additions method for measurement of surface-peptide retention affinities offers a number of significant advantages over conventional radiolabeled peptide binding methods and promises to be a valuable tool for the determination of this important biomaterial characteristic.
Walker
A K
AK
Department of Chemistry and Biochemistry, University of Texas at Arlington 76019-0065, USA.
Land
C M
CM
Kinsel
G R
GR
Nelson
K D
KD
D000327:Adsorption; D000803:Angiotensin I / Q000737:chemistry; D000818:Animals; D007328:Insulin / Q000737:chemistry; D007457:Iodine Radioisotopes / Q000737:chemistry; D007553:Isotope Labeling; D010455:Peptides / Q000737:chemistry*; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization; D013552:Swine
D007328:Insulin; D007457:Iodine Radioisotopes; D010455:Peptides; D000803:Angiotensin I