Next Issue
Previous Issue

Table of Contents

Antibodies, Volume 1, Issue 2 (September 2012), Pages 124-258

  • Issues are regarded as officially published after their release is announced to the table of contents alert mailing list.
  • You may sign up for e-mail alerts to receive table of contents of newly released issues.
  • PDF is the official format for papers published in both, html and pdf forms. To view the papers in pdf format, click on the "PDF Full-text" link, and use the free Adobe Readerexternal link to open them.
View options order results:
result details:
Displaying articles 1-6
Export citation of selected articles as:

Research

Jump to: Review

Open AccessArticle Dual Targeting of Tumor Cells with Bispecific Single-Chain Fv-Immunoliposomes
Antibodies 2012, 1(2), 199-214; doi:10.3390/antib1020199
Received: 8 May 2012 / Revised: 9 July 2012 / Accepted: 13 July 2012 / Published: 25 July 2012
Cited by 11 | PDF Full-text (799 KB) | HTML Full-text | XML Full-text
Abstract
Antibody fragments, especially single-chain Fv fragments, have been established for the generation of immunoliposomes for targeted drug delivery in cancer therapy and other applications. Bispecific immunoliposomes should be useful for dual targeting addressing inter- and intratumoral heterogeneity of tumor antigen expression. Here, we
[...] Read more.
Antibody fragments, especially single-chain Fv fragments, have been established for the generation of immunoliposomes for targeted drug delivery in cancer therapy and other applications. Bispecific immunoliposomes should be useful for dual targeting addressing inter- and intratumoral heterogeneity of tumor antigen expression. Here, we established a protocol to generate dual-targeted immunoliposomes using genetically engineered scFv molecules recognizing two different tumor-associated antigens, EGFR and CEA (CEACAM5), applying a step-wise insertion of antibody-coupled micelles into preformed PEGylated liposomes. The dual-targeted immunoliposomes retained binding activity for both antigens and combined the selectivity of both antibodies within one liposome. Thus, these dual-targeted immunoliposomes should be suitable to deliver therapeutic payloads to tumor cells expressing EGFR or CEA, or both antigens. Full article
(This article belongs to the Special Issue Bispecific Antibodies for Dual Targeting Strategies)
Figures

Review

Jump to: Research

Open AccessReview Alpha Particle Emitter Radiolabeled Antibody for Metastatic Cancer: What Can We Learn from Heavy Ion Beam Radiobiology?
Antibodies 2012, 1(2), 124-148; doi:10.3390/antib1020124
Received: 3 May 2012 / Revised: 17 June 2012 / Accepted: 20 June 2012 / Published: 26 June 2012
Cited by 1 | PDF Full-text (350 KB) | HTML Full-text | XML Full-text
Abstract
Alpha-particle emitter labeled monoclonal antibodies are being actively developed for treatment of metastatic cancer due to the high linear energy transfer (LET) and the resulting greater biological efficacy of alpha-emitters. Our knowledge of high LET particle radiobiology derives primarily from accelerated heavy ion
[...] Read more.
Alpha-particle emitter labeled monoclonal antibodies are being actively developed for treatment of metastatic cancer due to the high linear energy transfer (LET) and the resulting greater biological efficacy of alpha-emitters. Our knowledge of high LET particle radiobiology derives primarily from accelerated heavy ion beam studies. In heavy ion beam therapy of loco-regional tumors, the modulation of steep transition to very high LET peak as the particle approaches the end of its track (known as the Bragg peak) enables greater delivery of biologically potent radiation to the deep seated tumors while sparing normal tissues surrounding the tumor with the relatively low LET track segment part of the heavy ion beam. Moreover, fractionation of the heavy ion beam can further enhance the peak-to-plateau relative biological effectiveness (RBE) ratio. In contrast, internally delivered alpha particle radiopharmaceutical therapy lack the control of Bragg peak energy deposition and the dose rate is determined by the administered activity, alpha-emitter half-life and biological kinetics of the radiopharmaceutical. The therapeutic ratio of tumor to normal tissue is mainly achieved by tumor specific targeting of the carrier antibody. In this brief overview, we review the radiobiology of high LET radiations learned from ion beam studies and identify the features that are also applicable for the development of alpha-emitter labeled antibodies. The molecular mechanisms underlying DNA double strand break repair response to high LET radiation are also discussed. Full article
(This article belongs to the Special Issue Modes of Antibody Action for Cancer Therapy)
Open AccessReview Current and Potential Uses of Immunocytokines as Cancer Immunotherapy
Antibodies 2012, 1(2), 149-171; doi:10.3390/antib1020149
Received: 13 June 2012 / Revised: 26 June 2012 / Accepted: 26 June 2012 / Published: 4 July 2012
Cited by 12 | PDF Full-text (507 KB) | HTML Full-text | XML Full-text
Abstract
Immunocytokines (ICs) are a class of molecules created by linking tumor-reactive monoclonal antibodies to cytokines that are able to activate immune cells. Tumor selective localization is provided by the ability of the mAb component to bind to molecules found on the tumor cell
[...] Read more.
Immunocytokines (ICs) are a class of molecules created by linking tumor-reactive monoclonal antibodies to cytokines that are able to activate immune cells. Tumor selective localization is provided by the ability of the mAb component to bind to molecules found on the tumor cell surface or molecules found selectively in the tumor microenvronment. In this way the cytokine component of the immunocytokine is selectively localized to sites of tumor and can activate immune cells with appropriate receptors for the cytokine. Immunocytokines have been made and tested by us, and others, using a variety of tumor-reactive mAbs linked to distinct cytokines. To date, the majority of clinical progress has been made with ICs that have linked human interleukin-2 (IL2) to a select number of tumor reactive mAbs that had already been in prior clinical testing as non-modified mAbs. Here we briefly review the background for the creation of ICs, summarize current clinical progress, emphasize mechanisms of action for ICs that are distinct from those of their constituent components, and present some directions for future development and testing. Full article
(This article belongs to the Special Issue Modes of Antibody Action for Cancer Therapy)
Open AccessReview Cancer Immunotherapy by Retargeting of Immune Effector Cells via Recombinant Bispecific Antibody Constructs
Antibodies 2012, 1(2), 172-198; doi:10.3390/antib1020172
Received: 24 May 2012 / Revised: 27 June 2012 / Accepted: 10 July 2012 / Published: 18 July 2012
Cited by 12 | PDF Full-text (623 KB) | HTML Full-text | XML Full-text
Abstract
Immunotherapy has emerged as an alternative strategy to treat malignancies in addition to conventional radio- and chemotherapy. There has been a plethora of evidence that the immune system is able to control tumor outgrowth and a number of strategies have been put forward
[...] Read more.
Immunotherapy has emerged as an alternative strategy to treat malignancies in addition to conventional radio- and chemotherapy. There has been a plethora of evidence that the immune system is able to control tumor outgrowth and a number of strategies have been put forward to utilize this ability for immunotherapy. However, some of these strategies have not been very efficient and their success has been limited by tumor evasion mechanisms. A promising approach to engage effector cells of the immune system overcoming some of the escape mechanisms has been introduced more than two decades ago. This approach is based on bispecific antibodies. Here we summarize the evolution of bispecific antibodies, their improvement, remaining obstacles and some controversial reports. Full article
(This article belongs to the Special Issue Bispecific Antibodies for Dual Targeting Strategies)
Open AccessReview Refolding Technology for scFv Using a New Detergent, N-Lauroyl-L-glutamate and Arginine
Antibodies 2012, 1(2), 215-238; doi:10.3390/antib1020215
Received: 10 July 2012 / Revised: 16 August 2012 / Accepted: 21 August 2012 / Published: 29 August 2012
Cited by 1 | PDF Full-text (428 KB) | HTML Full-text | XML Full-text
Abstract
Monoclonal antibodies to the soluble antigens or cell surface markers hold great promise as effective human therapeutics. One of the major disadvantages is its large size, which prevents efficient penetration into the target tissues. Smaller version of antibodies, which has only antigen binding
[...] Read more.
Monoclonal antibodies to the soluble antigens or cell surface markers hold great promise as effective human therapeutics. One of the major disadvantages is its large size, which prevents efficient penetration into the target tissues. Smaller version of antibodies, which has only antigen binding sites, is extensively investigated. It becomes increasingly apparent, however, that these smaller fragments of antibodies are rather difficult to produce, as the normally efficient mammalian secretion system does not work well for these fragments. Thus, refolding of insoluble proteins produced in Escherichia coli is a method of choice, although such refolding is mainly based on trial-and-error experiment. Here we describe a novel refolding system using a new amino acid-based detergent, N-lauroyl-L-glutamate, and arginine. This detergent appears to readily dissociate from proteins below critical micelle concentration (CMC), while remaining effective in protein solubilization above CMC. Arginine suppresses protein aggregation when the detergent concentration was reduced below CMC. The interaction of the detergent and arginine with proteins, which play an important role in protein refolding, will be discussed in great length. Full article
Open AccessReview Fluobodies against Bioactive Natural Products and their Application in Fluorescence-Linked Immunosorbent Assay
Antibodies 2012, 1(2), 239-258; doi:10.3390/antib1020239
Received: 7 August 2012 / Revised: 27 August 2012 / Accepted: 28 August 2012 / Published: 11 September 2012
Cited by 7 | PDF Full-text (1074 KB) | HTML Full-text | XML Full-text
Abstract
An enzyme-linked immunosorbent assay (ELISA) using monoclonal antibody (MAb), Fab antibody, and single-chain variable fragment (scFv) antibody has become one of the most promising analytical methods owing to its rapidity, sensitivity, and reliability. Recently, a chimera of green fluorescent protein (GFP) with a
[...] Read more.
An enzyme-linked immunosorbent assay (ELISA) using monoclonal antibody (MAb), Fab antibody, and single-chain variable fragment (scFv) antibody has become one of the most promising analytical methods owing to its rapidity, sensitivity, and reliability. Recently, a chimera of green fluorescent protein (GFP) with a scFv antibody, named fluobody, was proposed as a probe for an alternative immunosorbent assay; i.e., fluorescence-linked immunosorbent assay (FLISA). In this FLISA, an even more sensitive, simple, and rapid immunoassay can be performed by detecting the highly sensitive fluorophore of GFP that is genetically and directly fused to the scFv antibody. In addition, the time- and cost-consuming secondary antibody reaction and the following enzyme-substrate reaction, necessary for conventional ELISA, can be avoided, making it possible to complete the assay more rapidly. Focusing on naturally occurring bioactive products, fluobody recognizing 1,4-naphthoquinone, plumbagin and triterpenoid saponin, ginsenosides were successfully expressed in Escherichia coli (E. coli) and applied to FLISA. The construction, the expression, and the potential use of fluobody in quantitative/qualitative analysis of bioactive natural products are reviewed in this article. Full article

Journal Contact

MDPI AG
Antibodies Editorial Office
St. Alban-Anlage 66, 4052 Basel, Switzerland
antibodies@mdpi.com
Tel. +41 61 683 77 34
Fax: +41 61 302 89 18
Editorial Board
Contact Details Submit to Antibodies
Back to Top