Pico- and femtosecond laser-induced crosslinking of protein microstructures: Evaluation of processability and bioactivity

Sanna Turunen, Elli Käpylä (Corresponding Author), Konstantina Terzaki, Jouko Viitanen, Costas Fotakis, Minna Kellomäki, Maria Farsari

Research output: Contribution to journalArticleScientificpeer-review

29 Citations (Scopus)

Abstract

This study reports the pico- and femtosecond laser-induced photocrosslinking of protein microstructures. The capabilities of a picosecond Nd:YAG laser to promote multiphoton excited crosslinking of proteins were evaluated by fabricating 2D and 3D microstructures of avidin, bovine serum albumin (BSA) and biotinylated bovine serum albumin (bBSA). The multiphoton absorption-induced photocrosslinking of proteins was demonstrated here for the first time with a non-toxic biomolecule flavin mononucleotide (FMN) as the photosensitizer. Sub-micrometer and micrometer scale structures were fabricated from several different compositions of protein and photosensitizer by varying the average laser power and scanning speed in order to determine the optimal process parameters for efficient photocrosslinking. In addition, the retention of ligand-binding ability of the crosslinked protein structures was shown by fluorescence imaging of immobilized biotin or streptavidin conjugated fluorescence labels. The surface topography and the resolution of the protein patterns fabricated with the Nd:YAG laser were compared to the results obtained with a femtosecond Ti:Sapphire laser. Quite similar grain characteristics and comparable feature sizes were achieved with both laser sources, which demonstrates the utility of the low-cost Nd:YAG microlaser for direct laser writing of protein microstructures.
Original languageEnglish
Article number045002
JournalBiofabrication
Volume3
Issue number4
DOIs
Publication statusPublished - 2011
MoE publication typeA1 Journal article-refereed

Fingerprint

Bioactivity
Ultrashort pulses
Crosslinking
Lasers
Proteins
Microstructure
Photosensitizing Agents
Photosensitizers
Solid-State Lasers
Bovine Serum Albumin
Fluorescence
Flavin Mononucleotide
Streptavidin
Avidin
Aluminum Oxide
Optical Imaging
Biomolecules
Surface topography
Biotin
Sapphire

Keywords

  • Laser
  • microstructures
  • Nd:YAG laser
  • fluorescence imaging
  • protein

Cite this

Turunen, S., Käpylä, E., Terzaki, K., Viitanen, J., Fotakis, C., Kellomäki, M., & Farsari, M. (2011). Pico- and femtosecond laser-induced crosslinking of protein microstructures: Evaluation of processability and bioactivity. Biofabrication, 3(4), [045002]. https://doi.org/10.1088/1758-5082/3/4/045002
Turunen, Sanna ; Käpylä, Elli ; Terzaki, Konstantina ; Viitanen, Jouko ; Fotakis, Costas ; Kellomäki, Minna ; Farsari, Maria. / Pico- and femtosecond laser-induced crosslinking of protein microstructures : Evaluation of processability and bioactivity. In: Biofabrication. 2011 ; Vol. 3, No. 4.
@article{e9099abb41a44971b2da3a851f188943,
title = "Pico- and femtosecond laser-induced crosslinking of protein microstructures: Evaluation of processability and bioactivity",
abstract = "This study reports the pico- and femtosecond laser-induced photocrosslinking of protein microstructures. The capabilities of a picosecond Nd:YAG laser to promote multiphoton excited crosslinking of proteins were evaluated by fabricating 2D and 3D microstructures of avidin, bovine serum albumin (BSA) and biotinylated bovine serum albumin (bBSA). The multiphoton absorption-induced photocrosslinking of proteins was demonstrated here for the first time with a non-toxic biomolecule flavin mononucleotide (FMN) as the photosensitizer. Sub-micrometer and micrometer scale structures were fabricated from several different compositions of protein and photosensitizer by varying the average laser power and scanning speed in order to determine the optimal process parameters for efficient photocrosslinking. In addition, the retention of ligand-binding ability of the crosslinked protein structures was shown by fluorescence imaging of immobilized biotin or streptavidin conjugated fluorescence labels. The surface topography and the resolution of the protein patterns fabricated with the Nd:YAG laser were compared to the results obtained with a femtosecond Ti:Sapphire laser. Quite similar grain characteristics and comparable feature sizes were achieved with both laser sources, which demonstrates the utility of the low-cost Nd:YAG microlaser for direct laser writing of protein microstructures.",
keywords = "Laser, microstructures, Nd:YAG laser, fluorescence imaging, protein",
author = "Sanna Turunen and Elli K{\"a}pyl{\"a} and Konstantina Terzaki and Jouko Viitanen and Costas Fotakis and Minna Kellom{\"a}ki and Maria Farsari",
note = "Project code: 23447",
year = "2011",
doi = "10.1088/1758-5082/3/4/045002",
language = "English",
volume = "3",
journal = "Biofabrication",
issn = "1758-5082",
publisher = "Institute of Physics IOP",
number = "4",

}

Turunen, S, Käpylä, E, Terzaki, K, Viitanen, J, Fotakis, C, Kellomäki, M & Farsari, M 2011, 'Pico- and femtosecond laser-induced crosslinking of protein microstructures: Evaluation of processability and bioactivity', Biofabrication, vol. 3, no. 4, 045002. https://doi.org/10.1088/1758-5082/3/4/045002

Pico- and femtosecond laser-induced crosslinking of protein microstructures : Evaluation of processability and bioactivity. / Turunen, Sanna; Käpylä, Elli (Corresponding Author); Terzaki, Konstantina; Viitanen, Jouko; Fotakis, Costas; Kellomäki, Minna; Farsari, Maria.

In: Biofabrication, Vol. 3, No. 4, 045002, 2011.

Research output: Contribution to journalArticleScientificpeer-review

TY - JOUR

T1 - Pico- and femtosecond laser-induced crosslinking of protein microstructures

T2 - Evaluation of processability and bioactivity

AU - Turunen, Sanna

AU - Käpylä, Elli

AU - Terzaki, Konstantina

AU - Viitanen, Jouko

AU - Fotakis, Costas

AU - Kellomäki, Minna

AU - Farsari, Maria

N1 - Project code: 23447

PY - 2011

Y1 - 2011

N2 - This study reports the pico- and femtosecond laser-induced photocrosslinking of protein microstructures. The capabilities of a picosecond Nd:YAG laser to promote multiphoton excited crosslinking of proteins were evaluated by fabricating 2D and 3D microstructures of avidin, bovine serum albumin (BSA) and biotinylated bovine serum albumin (bBSA). The multiphoton absorption-induced photocrosslinking of proteins was demonstrated here for the first time with a non-toxic biomolecule flavin mononucleotide (FMN) as the photosensitizer. Sub-micrometer and micrometer scale structures were fabricated from several different compositions of protein and photosensitizer by varying the average laser power and scanning speed in order to determine the optimal process parameters for efficient photocrosslinking. In addition, the retention of ligand-binding ability of the crosslinked protein structures was shown by fluorescence imaging of immobilized biotin or streptavidin conjugated fluorescence labels. The surface topography and the resolution of the protein patterns fabricated with the Nd:YAG laser were compared to the results obtained with a femtosecond Ti:Sapphire laser. Quite similar grain characteristics and comparable feature sizes were achieved with both laser sources, which demonstrates the utility of the low-cost Nd:YAG microlaser for direct laser writing of protein microstructures.

AB - This study reports the pico- and femtosecond laser-induced photocrosslinking of protein microstructures. The capabilities of a picosecond Nd:YAG laser to promote multiphoton excited crosslinking of proteins were evaluated by fabricating 2D and 3D microstructures of avidin, bovine serum albumin (BSA) and biotinylated bovine serum albumin (bBSA). The multiphoton absorption-induced photocrosslinking of proteins was demonstrated here for the first time with a non-toxic biomolecule flavin mononucleotide (FMN) as the photosensitizer. Sub-micrometer and micrometer scale structures were fabricated from several different compositions of protein and photosensitizer by varying the average laser power and scanning speed in order to determine the optimal process parameters for efficient photocrosslinking. In addition, the retention of ligand-binding ability of the crosslinked protein structures was shown by fluorescence imaging of immobilized biotin or streptavidin conjugated fluorescence labels. The surface topography and the resolution of the protein patterns fabricated with the Nd:YAG laser were compared to the results obtained with a femtosecond Ti:Sapphire laser. Quite similar grain characteristics and comparable feature sizes were achieved with both laser sources, which demonstrates the utility of the low-cost Nd:YAG microlaser for direct laser writing of protein microstructures.

KW - Laser

KW - microstructures

KW - Nd:YAG laser

KW - fluorescence imaging

KW - protein

U2 - 10.1088/1758-5082/3/4/045002

DO - 10.1088/1758-5082/3/4/045002

M3 - Article

VL - 3

JO - Biofabrication

JF - Biofabrication

SN - 1758-5082

IS - 4

M1 - 045002

ER -