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Interaction of polyamidoamine (PAMAM) succinamic acid dendrimers generation 4 with human serum albumin

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Title: Interaction of polyamidoamine (PAMAM) succinamic acid dendrimers generation 4 with human serum albumin
Authors: Sekowski, Szymon1 sekowski100@vp.pl, Buczkowski, Adam2, Palecz, Bartlomiej2, Gabryelak, Teresa1
Source: Spectrochimica Acta Part A: Molecular & Biomolecular Spectroscopy. Oct2011, Vol. 81 Issue 1, p706-710. 5p.
Subjects: Polyamines, Carboxylic acids, Dendrimers, Serum albumin, Fluorescence spectroscopy, Circular dichroism, Protein structure, Calorimetry
Abstract: Abstract: Dendrimers, a relatively new group of highly branched three dimensional polymers, are intensively investigated to use them in biomedical and physicochemical sciences. Their specific architecture gives them the ability to interact with many different types of molecules. In our studies the interaction between PAMAM succinamic acid dendrimers generation 4 (PAMAM-SAH G4) and human serum albumin (HSA) was examined. Experiments showed that a single molecule of a HSA can bind approximately 6 particles of dendrimers. The fluorescence studies demonstrated that dendrimers lead to a decrease in protein fluorescence but changes in fluorescence anisotropy were not observed. Alterations in the spectrum of circular dichroism indicated changes in the secondary protein structure. The results clearly show that this generation of dendrimers possesses a strong ability to interact with human serum albumin. [Copyright &y& Elsevier]
Copyright of Spectrochimica Acta Part A: Molecular & Biomolecular Spectroscopy is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract. (Copyright applies to all Abstracts.)
Database: Engineering Source
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  Availability: 0
Header DbId: egs
DbLabel: Engineering Source
An: 65501289
AccessLevel: 6
PubType: Academic Journal
PubTypeId: academicJournal
PreciseRelevancyScore: 0
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  Label: Title
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  Data: Interaction of polyamidoamine (PAMAM) succinamic acid dendrimers generation 4 with human serum albumin
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  Data: <searchLink fieldCode="JN" term="%22Spectrochimica+Acta+Part+A%3A+Molecular+%26+Biomolecular+Spectroscopy%22">Spectrochimica Acta Part A: Molecular & Biomolecular Spectroscopy</searchLink>. Oct2011, Vol. 81 Issue 1, p706-710. 5p.
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  Data: <searchLink fieldCode="DE" term="%22Polyamines%22">Polyamines</searchLink><br /><searchLink fieldCode="DE" term="%22Carboxylic+acids%22">Carboxylic acids</searchLink><br /><searchLink fieldCode="DE" term="%22Dendrimers%22">Dendrimers</searchLink><br /><searchLink fieldCode="DE" term="%22Serum+albumin%22">Serum albumin</searchLink><br /><searchLink fieldCode="DE" term="%22Fluorescence+spectroscopy%22">Fluorescence spectroscopy</searchLink><br /><searchLink fieldCode="DE" term="%22Circular+dichroism%22">Circular dichroism</searchLink><br /><searchLink fieldCode="DE" term="%22Protein+structure%22">Protein structure</searchLink><br /><searchLink fieldCode="DE" term="%22Calorimetry%22">Calorimetry</searchLink>
– Name: Abstract
  Label: Abstract
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  Data: Abstract: Dendrimers, a relatively new group of highly branched three dimensional polymers, are intensively investigated to use them in biomedical and physicochemical sciences. Their specific architecture gives them the ability to interact with many different types of molecules. In our studies the interaction between PAMAM succinamic acid dendrimers generation 4 (PAMAM-SAH G4) and human serum albumin (HSA) was examined. Experiments showed that a single molecule of a HSA can bind approximately 6 particles of dendrimers. The fluorescence studies demonstrated that dendrimers lead to a decrease in protein fluorescence but changes in fluorescence anisotropy were not observed. Alterations in the spectrum of circular dichroism indicated changes in the secondary protein structure. The results clearly show that this generation of dendrimers possesses a strong ability to interact with human serum albumin. [Copyright &y& Elsevier]
– Name: AbstractSuppliedCopyright
  Label:
  Group: Ab
  Data: <i>Copyright of Spectrochimica Acta Part A: Molecular & Biomolecular Spectroscopy is the property of Elsevier B.V. and its content may not be copied or emailed to multiple sites without the copyright holder's express written permission. Additionally, content may not be used with any artificial intelligence tools or machine learning technologies. However, users may print, download, or email articles for individual use. This abstract may be abridged. No warranty is given about the accuracy of the copy. Users should refer to the original published version of the material for the full abstract.</i> (Copyright applies to all Abstracts.)
PLink https://search.ebscohost.com/login.aspx?direct=true&site=eds-live&db=egs&AN=65501289
RecordInfo BibRecord:
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      – Type: doi
        Value: 10.1016/j.saa.2011.07.009
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      – Code: eng
        Text: English
    PhysicalDescription:
      Pagination:
        PageCount: 5
        StartPage: 706
    Subjects:
      – SubjectFull: Polyamines
        Type: general
      – SubjectFull: Carboxylic acids
        Type: general
      – SubjectFull: Dendrimers
        Type: general
      – SubjectFull: Serum albumin
        Type: general
      – SubjectFull: Fluorescence spectroscopy
        Type: general
      – SubjectFull: Circular dichroism
        Type: general
      – SubjectFull: Protein structure
        Type: general
      – SubjectFull: Calorimetry
        Type: general
    Titles:
      – TitleFull: Interaction of polyamidoamine (PAMAM) succinamic acid dendrimers generation 4 with human serum albumin
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            NameFull: Sekowski, Szymon
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            NameFull: Buczkowski, Adam
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            NameFull: Palecz, Bartlomiej
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            NameFull: Gabryelak, Teresa
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              Text: Oct2011
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              Y: 2011
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