Adsorption behavior of linear and cyclic genetically engineered platinum binding peptides

Urartu Ozgur Safak Seker, Brandon Wilson, Sevil Dincer, Il Won Kim, Ersin Emre Oren, John Evans, Candan Tamerler, Mehmet Sarikaya

Research output: Contribution to journalArticle

Abstract

Recently, phage and cell-surface display libraries have been adapted for genetically selecting short peptides for a variety of inorganic materials. Despite the enormous number of inorganic-binding peptides reported and their bionanotechnological utility as synthesizers and molecular linkers, there is still a limited understanding of molecular mechanisms of peptide recognition of and binding to solid materials. As part of our goal of genetically designing these peptides, understanding the binding kinetics and thermodynamics, and using the peptides as molecular erectors, in this report we discuss molecular structural constraints imposed upon the quantitative binding characteristics of peptides with an affinity for inorganics. Specifically, we use a high-affinity seven amino acid Pt-binding sequence, PTSTGQA, as we reported in earlier studies and build two constructs: one is a Cys-Cys constrained "loop" sequence (CPTSTGQAC) that mimics the domain used in the pill tail sequence of the phage library construction, and the second is the linear form, a septapeptide, without the loop. Both sequences were analyzed for their adsorption behavior on Pt thin films by surface plasmon resonance (SPR) spectroscopy and for their conformational properties by circular dichroism (CD). We find that the cyclic peptide of the integral Pt-binding sequence possesses single or 1:1 Langmuir adsorption behavior and displays equilibrium and adsorption rate constants that are significantly larger than those obtained for the linear form. Conversely, the linear form exhibits biexponential Langmuir isotherm behavior with slower and weaker binding. Furthermore, the structure of the cyclic version was found to adopt a random coil molecular conformation, whereas the linear version adopts a polyproline type II conformation in equilibrium with the random coil. The 2,2,2-trifluoroethanol titration experiments indicate that TFE has a different effect on the secondary structures of the linear and cyclic versions of the Pt binding sequence. We conclude that the presence of the Cys-Cys restraint affects both the conformation and binding behavior of the integral Pt-binding septapeptide sequence and that the presence or absence of constraints could be used to tune the adsorption and structural features of inorganic binding peptide sequences.

Original languageEnglish (US)
Pages (from-to)7895-7900
Number of pages6
JournalLangmuir
Volume23
Issue number15
DOIs
StatePublished - Jul 17 2007

Fingerprint

Platinum
Peptides
peptides
platinum
Adsorption
adsorption
Conformations
Bacteriophages
Trifluoroethanol
Cyclic Peptides
affinity
Polytetrafluoroethylene
Dichroism
Surface plasmon resonance
coils
Titration
Isotherms
Amino acids
Rate constants
synthesizers

ASJC Scopus subject areas

  • Physical and Theoretical Chemistry
  • Colloid and Surface Chemistry

Cite this

Seker, U. O. S., Wilson, B., Dincer, S., Kim, I. W., Oren, E. E., Evans, J., ... Sarikaya, M. (2007). Adsorption behavior of linear and cyclic genetically engineered platinum binding peptides. Langmuir, 23(15), 7895-7900. https://doi.org/10.1021/la700446g

Adsorption behavior of linear and cyclic genetically engineered platinum binding peptides. / Seker, Urartu Ozgur Safak; Wilson, Brandon; Dincer, Sevil; Kim, Il Won; Oren, Ersin Emre; Evans, John; Tamerler, Candan; Sarikaya, Mehmet.

In: Langmuir, Vol. 23, No. 15, 17.07.2007, p. 7895-7900.

Research output: Contribution to journalArticle

Seker, UOS, Wilson, B, Dincer, S, Kim, IW, Oren, EE, Evans, J, Tamerler, C & Sarikaya, M 2007, 'Adsorption behavior of linear and cyclic genetically engineered platinum binding peptides', Langmuir, vol. 23, no. 15, pp. 7895-7900. https://doi.org/10.1021/la700446g
Seker, Urartu Ozgur Safak ; Wilson, Brandon ; Dincer, Sevil ; Kim, Il Won ; Oren, Ersin Emre ; Evans, John ; Tamerler, Candan ; Sarikaya, Mehmet. / Adsorption behavior of linear and cyclic genetically engineered platinum binding peptides. In: Langmuir. 2007 ; Vol. 23, No. 15. pp. 7895-7900.
@article{173ce73b7722472989e36211bd74c60f,
title = "Adsorption behavior of linear and cyclic genetically engineered platinum binding peptides",
abstract = "Recently, phage and cell-surface display libraries have been adapted for genetically selecting short peptides for a variety of inorganic materials. Despite the enormous number of inorganic-binding peptides reported and their bionanotechnological utility as synthesizers and molecular linkers, there is still a limited understanding of molecular mechanisms of peptide recognition of and binding to solid materials. As part of our goal of genetically designing these peptides, understanding the binding kinetics and thermodynamics, and using the peptides as molecular erectors, in this report we discuss molecular structural constraints imposed upon the quantitative binding characteristics of peptides with an affinity for inorganics. Specifically, we use a high-affinity seven amino acid Pt-binding sequence, PTSTGQA, as we reported in earlier studies and build two constructs: one is a Cys-Cys constrained {"}loop{"} sequence (CPTSTGQAC) that mimics the domain used in the pill tail sequence of the phage library construction, and the second is the linear form, a septapeptide, without the loop. Both sequences were analyzed for their adsorption behavior on Pt thin films by surface plasmon resonance (SPR) spectroscopy and for their conformational properties by circular dichroism (CD). We find that the cyclic peptide of the integral Pt-binding sequence possesses single or 1:1 Langmuir adsorption behavior and displays equilibrium and adsorption rate constants that are significantly larger than those obtained for the linear form. Conversely, the linear form exhibits biexponential Langmuir isotherm behavior with slower and weaker binding. Furthermore, the structure of the cyclic version was found to adopt a random coil molecular conformation, whereas the linear version adopts a polyproline type II conformation in equilibrium with the random coil. The 2,2,2-trifluoroethanol titration experiments indicate that TFE has a different effect on the secondary structures of the linear and cyclic versions of the Pt binding sequence. We conclude that the presence of the Cys-Cys restraint affects both the conformation and binding behavior of the integral Pt-binding septapeptide sequence and that the presence or absence of constraints could be used to tune the adsorption and structural features of inorganic binding peptide sequences.",
author = "Seker, {Urartu Ozgur Safak} and Brandon Wilson and Sevil Dincer and Kim, {Il Won} and Oren, {Ersin Emre} and John Evans and Candan Tamerler and Mehmet Sarikaya",
year = "2007",
month = "7",
day = "17",
doi = "10.1021/la700446g",
language = "English (US)",
volume = "23",
pages = "7895--7900",
journal = "Langmuir",
issn = "0743-7463",
publisher = "American Chemical Society",
number = "15",

}

TY - JOUR

T1 - Adsorption behavior of linear and cyclic genetically engineered platinum binding peptides

AU - Seker, Urartu Ozgur Safak

AU - Wilson, Brandon

AU - Dincer, Sevil

AU - Kim, Il Won

AU - Oren, Ersin Emre

AU - Evans, John

AU - Tamerler, Candan

AU - Sarikaya, Mehmet

PY - 2007/7/17

Y1 - 2007/7/17

N2 - Recently, phage and cell-surface display libraries have been adapted for genetically selecting short peptides for a variety of inorganic materials. Despite the enormous number of inorganic-binding peptides reported and their bionanotechnological utility as synthesizers and molecular linkers, there is still a limited understanding of molecular mechanisms of peptide recognition of and binding to solid materials. As part of our goal of genetically designing these peptides, understanding the binding kinetics and thermodynamics, and using the peptides as molecular erectors, in this report we discuss molecular structural constraints imposed upon the quantitative binding characteristics of peptides with an affinity for inorganics. Specifically, we use a high-affinity seven amino acid Pt-binding sequence, PTSTGQA, as we reported in earlier studies and build two constructs: one is a Cys-Cys constrained "loop" sequence (CPTSTGQAC) that mimics the domain used in the pill tail sequence of the phage library construction, and the second is the linear form, a septapeptide, without the loop. Both sequences were analyzed for their adsorption behavior on Pt thin films by surface plasmon resonance (SPR) spectroscopy and for their conformational properties by circular dichroism (CD). We find that the cyclic peptide of the integral Pt-binding sequence possesses single or 1:1 Langmuir adsorption behavior and displays equilibrium and adsorption rate constants that are significantly larger than those obtained for the linear form. Conversely, the linear form exhibits biexponential Langmuir isotherm behavior with slower and weaker binding. Furthermore, the structure of the cyclic version was found to adopt a random coil molecular conformation, whereas the linear version adopts a polyproline type II conformation in equilibrium with the random coil. The 2,2,2-trifluoroethanol titration experiments indicate that TFE has a different effect on the secondary structures of the linear and cyclic versions of the Pt binding sequence. We conclude that the presence of the Cys-Cys restraint affects both the conformation and binding behavior of the integral Pt-binding septapeptide sequence and that the presence or absence of constraints could be used to tune the adsorption and structural features of inorganic binding peptide sequences.

AB - Recently, phage and cell-surface display libraries have been adapted for genetically selecting short peptides for a variety of inorganic materials. Despite the enormous number of inorganic-binding peptides reported and their bionanotechnological utility as synthesizers and molecular linkers, there is still a limited understanding of molecular mechanisms of peptide recognition of and binding to solid materials. As part of our goal of genetically designing these peptides, understanding the binding kinetics and thermodynamics, and using the peptides as molecular erectors, in this report we discuss molecular structural constraints imposed upon the quantitative binding characteristics of peptides with an affinity for inorganics. Specifically, we use a high-affinity seven amino acid Pt-binding sequence, PTSTGQA, as we reported in earlier studies and build two constructs: one is a Cys-Cys constrained "loop" sequence (CPTSTGQAC) that mimics the domain used in the pill tail sequence of the phage library construction, and the second is the linear form, a septapeptide, without the loop. Both sequences were analyzed for their adsorption behavior on Pt thin films by surface plasmon resonance (SPR) spectroscopy and for their conformational properties by circular dichroism (CD). We find that the cyclic peptide of the integral Pt-binding sequence possesses single or 1:1 Langmuir adsorption behavior and displays equilibrium and adsorption rate constants that are significantly larger than those obtained for the linear form. Conversely, the linear form exhibits biexponential Langmuir isotherm behavior with slower and weaker binding. Furthermore, the structure of the cyclic version was found to adopt a random coil molecular conformation, whereas the linear version adopts a polyproline type II conformation in equilibrium with the random coil. The 2,2,2-trifluoroethanol titration experiments indicate that TFE has a different effect on the secondary structures of the linear and cyclic versions of the Pt binding sequence. We conclude that the presence of the Cys-Cys restraint affects both the conformation and binding behavior of the integral Pt-binding septapeptide sequence and that the presence or absence of constraints could be used to tune the adsorption and structural features of inorganic binding peptide sequences.

UR - http://www.scopus.com/inward/record.url?scp=34547239512&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=34547239512&partnerID=8YFLogxK

U2 - 10.1021/la700446g

DO - 10.1021/la700446g

M3 - Article

VL - 23

SP - 7895

EP - 7900

JO - Langmuir

JF - Langmuir

SN - 0743-7463

IS - 15

ER -