{"database":"biostudies-literature","file_versions":[],"scores":null,"additional":{"submitter":["Hinson CM"],"funding":["NICHD NIH HHS","NIDDK NIH HHS","Foundation for the National Institutes of Health","Welch Foundation","Welch Regents Chair","NIGMS NIH HHS","National Science Foundation"],"pagination":["14856-14865"],"full_dataset_link":["https://www.ebi.ac.uk/biostudies/studies/S-EPMC8982273"],"repository":["biostudies-literature"],"omics_type":["Unknown"],"volume":["37(51)"],"pubmed_abstract":["Silica passivating agents have shown great success in minimizing nonspecific protein binding to glass surfaces for imaging and microscopy applications. Amine-derivatized surfaces are commonly used in conjugation with amide coupling agents to immobilize peptides/proteins through C-terminal or side-chain carboxylic acids. In the case of the single-molecule fluorosequencing of peptides, attachment occurs via the C-terminus and nonspecific surface binding has previously been a source of error in peptide identification. Here, we employ fluorosequencing as a high-throughput, single-molecule sensitivity assay to identify and quantify the extent of nonspecific binding of peptides to amine-derivatized surfaces. We show that there is little improvement when using common passivating agents in combina"],"journal":["Langmuir : the ACS journal of surfaces and colloids"],"pubmed_title":["Studies of Surface Preparation for the Fluorosequencing of Peptides."],"pmcid":["PMC8982273"],"funding_grant_id":["R01 DK110520","F-0046","F-1515","R35 GM122480","STTR Grant #1938726","R01 HD085901"],"pubmed_authors":["Hinson CM","Swaminathan J","Anslyn EV","Shannon CE","Rivera S","Bardo AM","Marcotte EM"],"additional_accession":[]},"is_claimable":false,"name":"Studies of Surface Preparation for the Fluorosequencing of Peptides.","description":"Silica passivating agents have shown great success in minimizing nonspecific protein binding to glass surfaces for imaging and microscopy applications. Amine-derivatized surfaces are commonly used in conjugation with amide coupling agents to immobilize peptides/proteins through C-terminal or side-chain carboxylic acids. In the case of the single-molecule fluorosequencing of peptides, attachment occurs via the C-terminus and nonspecific surface binding has previously been a source of error in peptide identification. Here, we employ fluorosequencing as a high-throughput, single-molecule sensitivity assay to identify and quantify the extent of nonspecific binding of peptides to amine-derivatized surfaces. We show that there is little improvement when using common passivating agents in combina","dates":{"release":"2021-01-01T00:00:00Z","publication":"2021 Dec","modification":"2026-05-09T16:28:41.386Z","creation":"2025-04-05T22:18:29.48Z"},"accession":"S-EPMC8982273","cross_references":{"pubmed":["34904833"],"doi":["10.1021/acs.langmuir.1c02644"]}}