The use of dedicated peptide libraries permits the discovery of high affinity binding peptides

Dekoster, Hs; Amons, Reinout; Benckhuijsen, Willemien E.; Feijlbrief, M.; Schellekens, Gerard A.; Drijfhout, Jan W.

doi:10.1016/0022-1759(95)00182-a

Cited by 44 publications

(32 citation statements)

References 17 publications

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“…Second, comparison of the bactericidal activities of hLF(1-11) and peptides lacking one or more of the first 5 residues revealed that the first 2 arginines are essential for killing of bacteria. In agreement with these in vitro data, we found that hLF(1-11) was much more effective than hLF (4)(5)(6)(7)(8)(9)(10)(11) in reducing the number of viable bacteria in antibiotic-resistant S. aureus-infected as well as K. pneumoniaeinfected mice.…”

Section: ϫ3nsupporting

confidence: 88%

“…was applied instead of hLF or hLF Ϫ3N . Synthetic peptides corresponding to residues 1 to 11 of hLF (GRRRRSVQWCA, 1,494 Da), referred to below as hLF (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11), and fragments thereof and a peptide corresponding to residues 21 to 31 of hLF (FQWQRN MRKVR, 1,567 Da), referred to below as hLF (21)(22)(23)(24)(25)(26)(27)(28)(29)(30)(31), were prepared and purified as described previously (4). The purity of the synthetic peptides usually exceeded 88%, as determined by reverse-phase high-performance liquid chromatography.…”

Section: Methodsmentioning

confidence: 99%

“…Within 24 h after injection of natural hLF, hLF Ϫ3N , hLF(1-11), hLF(4-11), or hLF (21)(22)(23)(24)(25)(26)(27)(28)(29)(30)(31), the number of viable bacteria in mice infected with antibiotic-resistant S. aureus was reduced in a dose-dependent fashion; maximum effects were seen with 1 nmol of hLF, 10 nmol of hLF Ϫ3N , 0.1 nmol of hLF (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11), and 10 nmol of hLF (21)(22)(23)(24)(25)(26)(27)(28)(29)(30)(31) (Fig. 4).…”

Section: Fig 2 Killing Of Antibiotic-resistant S Aureus (A) L Momentioning

confidence: 99%

“…Accumulation of radiolabeled hLF, hLF Ϫ3N , hLF (1)(2)(3)(4)(5)(6)(7)(8)(9)(10)(11), hLF(4-11), or hLF(21-31) and, as a control, IgG at the site of infection in mice with an experimental thigh muscle infection with antibiotic-resistant S. aureus at various intervals after injection of radiolabeled protein or peptide is represented by the ratio of the radioactivity counts in identical ROI drawn over the infected (target, T) and the noninfected thigh muscle (nontarget, NT). Results (T/NT ratios) are means and standard deviations for at least three mice.…”

Section: Fig 5 Accumulation Ofmentioning

confidence: 99%

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Human Lactoferrin and Peptides Derived from Its N Terminus Are Highly Effective against Infections with Antibiotic-Resistant Bacteria

et al. 2001

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Since human lactoferrin (hLF) binds to bacterial products through its highly positively charged N terminus, we investigated which of the two cationic domains is involved in its bactericidal activity. The results revealed that hLF lacking the first three residues (hLF ؊3N ) was less efficient than hLF in killing of antibiotic-resistant Staphylococcus aureus, Listeria monocytogenes, and Klebsiella pneumoniae. Both hLF preparations failed to kill Escherichia coli O54. In addition, hLF ؊3N was less effective than hLF in reducing the number of viable bacteria in mice infected with antibiotic-resistant S. aureus and K. pneumoniae. Studies with synthetic peptides corresponding to the first 11 N-terminal amino acids, designated hLF(1-11), and fragments thereof demonstrated that peptides lacking the first three N-terminal residues are less effective than hLF(1-11) in killing of bacteria. Furthermore, a peptide corresponding to residues 21 to 31, which comprises the second cationic domain, was less effective than hLF(1-11) in killing of bacteria in vitro and in mice having an infection with antibioticresistant S. aureus or K. pneumoniae. Using fluorescent probes, we found that bactericidal hLF peptides, but not nonbactericidal peptides, caused an increase of the membrane permeability. In addition, hLF killed the various bacteria, most probably by inducing intracellular changes in these bacteria without affecting the membrane permeability. Together, hLF and peptides derived from its N terminus are highly effective against infections with antibiotic-resistant S. aureus and K. pneumoniae, and the first two arginines play an essential role in this activity.

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Section: ϫ3nsupporting

confidence: 88%

Section: Methodsmentioning

confidence: 99%

Section: Fig 2 Killing Of Antibiotic-resistant S Aureus (A) L Momentioning

confidence: 99%

Section: Fig 5 Accumulation Ofmentioning

confidence: 99%

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Human Lactoferrin and Peptides Derived from Its N Terminus Are Highly Effective against Infections with Antibiotic-Resistant Bacteria

et al. 2001

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“…Ceratotoxins were analyzed by laser desorption time-of-flight mass spectrometry with a Lasermat mass spectrometer (Finnigan MAT) according to the method of De Koster et al (1995).…”

Section: Methodsmentioning

confidence: 99%

Molecular Characterization of Ceratotoxin C, a Novel Antibacterial Female‐Specific Peptide of the Ceratotoxin Family from the Medfly Ceratitis Capitata

Rosetto¹,

Manetti²,

Giordano³

et al. 1996

European Journal of Biochemistry

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Ceratotoxins A and B are antibacterial peptides produced by the sexually mature females of Cerutitis capitata. The gene expression is restricted to the female reproductive accessory glands, and is not affected by bacterial infection, but is enhanced by mating. We report here the purification and the amino acid sequence of ceratotoxin C, a novel member of the ceratotoxin family, the cloning of its cDNA and the analysis of its expression. Ceratotoxin C is coordinately expressed with the other members of the ceratotoxin family. Its antibacterial activity is directed against both Gram-negative and Gram-positive bacterial strains but it is lower than that of ceratotoxin A. We demonstrate in the genome of C. capitata the presence of at least three ceratotoxin genes which express, in the female accessory glands, a set of peptides presumably involved in the protection of the genital tract during fertilization.

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A new hybrid resin for stepwise screening of peptide libraries combined with single bead Edman sequencing

et al. 1998

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A library system was developed for the discovery of bioactive peptides. Library synthesis and peptide sequencing was performed on a solid support while the screening for bioactivity was done with peptides in solution. The peptides were synthesized by split and mix, one-bead-one-peptide library synthesis, using a Tentagel S-NH2 solid support with a loading of approximately 100 pmol/bead. The major part of the peptide was connected to the support by a single acid-labile linker and a minor part of the peptide was acid-stabile attached to the polymer. The percentage of acid-stabile attached peptides could easily be controlled during modification of the amino functionalities of the resin at the start of the process. The cleavage rate of the acid-labile attached peptide from the resin depends on the composition of the cleavage mixture. When cleavage conditions were carefully controlled, a three-step partial cleavage protocol allowed for convergent bioactivity screening on peptide libraries using only one type of acid-labile linker. The partial cleavage and convergent screening procedure was repeated three times, after which the bead containing the bioactive peptide was sequenced. As such a bead still contained acid-stabile attached peptide, the Edman sequencing was straightforward and repetitive yields were excellent because the immobilized peptide was not washed out.

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The use of dedicated peptide libraries permits the discovery of high affinity binding peptides

Cited by 44 publications

References 17 publications

Human Lactoferrin and Peptides Derived from Its N Terminus Are Highly Effective against Infections with Antibiotic-Resistant Bacteria

Human Lactoferrin and Peptides Derived from Its N Terminus Are Highly Effective against Infections with Antibiotic-Resistant Bacteria

Molecular Characterization of Ceratotoxin C, a Novel Antibacterial Female‐Specific Peptide of the Ceratotoxin Family from the Medfly Ceratitis Capitata

A new hybrid resin for stepwise screening of peptide libraries combined with single bead Edman sequencing

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