Layer formation of a lipid-taged single-chain antibody and the interaction with antigen

Inger Vikholm; Jouko Peltonen

doi:10.1016/S0040-6090(95)08481-9

Layer formation of a lipid-taged single-chain antibody and the interaction with antigen

Inger Vikholm^*
, Jouko Peltonen

^*Corresponding author for this work

VTT Technical Research Centre of Finland

Åbo Akademi University

Research output: Contribution to journal › Article › Scientific › peer-review

7 Citations (Scopus)

Abstract

A phospholipid monolayer was prepared at the air-water interface and different amounts of a lipid-tagged genetically fragmented antibody were incorporated into the lipid matrix. The molecular surface area of the film increased with antibody concentration and reached a maximum at an antibody mole fraction of 0.03. Atomic force microscopy showed that the antibody fragment was segregated into protein-rich domains with a mean diameter of about 12 nm. In-situ measurements with surface plasmon resonance displayed a specific binding of antigen—a binding that was not observed to the pure lipid film.

Original language	English
Pages (from-to)	924-926
Journal	Thin Solid Films
Volume	284-285
DOIs	https://doi.org/10.1016/S0040-6090(95)08481-9
Publication status	Published - 1996
MoE publication type	A1 Journal article-refereed
Event	Seventh International Conference on Organized Molecular Films - Numana, Italy Duration: 10 Sept 1995 → 15 Sept 1995

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10.1016/S0040-6090(95)08481-9

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title = "Layer formation of a lipid-taged single-chain antibody and the interaction with antigen",

abstract = "A phospholipid monolayer was prepared at the air-water interface and different amounts of a lipid-tagged genetically fragmented antibody were incorporated into the lipid matrix. The molecular surface area of the film increased with antibody concentration and reached a maximum at an antibody mole fraction of 0.03. Atomic force microscopy showed that the antibody fragment was segregated into protein-rich domains with a mean diameter of about 12 nm. In-situ measurements with surface plasmon resonance displayed a specific binding of antigen—a binding that was not observed to the pure lipid film.",

author = "Inger Vikholm and Jouko Peltonen",

note = "Project code: KET4245; Seventh International Conference on Organized Molecular Films ; Conference date: 10-09-1995 Through 15-09-1995",

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doi = "10.1016/S0040-6090(95)08481-9",

language = "English",

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journal = "Thin Solid Films",

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AU - Vikholm, Inger

AU - Peltonen, Jouko

N1 - Project code: KET4245

PY - 1996

Y1 - 1996

N2 - A phospholipid monolayer was prepared at the air-water interface and different amounts of a lipid-tagged genetically fragmented antibody were incorporated into the lipid matrix. The molecular surface area of the film increased with antibody concentration and reached a maximum at an antibody mole fraction of 0.03. Atomic force microscopy showed that the antibody fragment was segregated into protein-rich domains with a mean diameter of about 12 nm. In-situ measurements with surface plasmon resonance displayed a specific binding of antigen—a binding that was not observed to the pure lipid film.

AB - A phospholipid monolayer was prepared at the air-water interface and different amounts of a lipid-tagged genetically fragmented antibody were incorporated into the lipid matrix. The molecular surface area of the film increased with antibody concentration and reached a maximum at an antibody mole fraction of 0.03. Atomic force microscopy showed that the antibody fragment was segregated into protein-rich domains with a mean diameter of about 12 nm. In-situ measurements with surface plasmon resonance displayed a specific binding of antigen—a binding that was not observed to the pure lipid film.

U2 - 10.1016/S0040-6090(95)08481-9

DO - 10.1016/S0040-6090(95)08481-9

M3 - Article

SN - 0040-6090

VL - 284-285

SP - 924

EP - 926

JO - Thin Solid Films

JF - Thin Solid Films

T2 - Seventh International Conference on Organized Molecular Films

Y2 - 10 September 1995 through 15 September 1995

ER -

Layer formation of a lipid-taged single-chain antibody and the interaction with antigen

Abstract

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