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Intrabody Communication Using Contact Electrodes in Low-Frequency Bands
Published in Daniel Tze Huei Lai, Rezaul Begg, Marimuthu Palaniswami, Healthcare Sensor Networks, 2016
Ken Sasaki, Fukuro Koshiji, Shudo Takenaka
Intrabody communication is a wireless communication method that utilizes a part of the human body as a transmission medium. It is considered one of the options for data communications between wearable devices and peripheral devices. Networks containing these devices are called body area networks (BANs) or body-centric networks. One of the primary application fields for BANs is healthcare monitoring systems, because multiple wearable sensors have to be connected wirelessly to collect the patient’s vital data.
SpyDisplay: A versatile phage display selection system using SpyTag/SpyCatcher technology
Published in mAbs, 2023
Sarah-Jane Kellmann, Christian Hentrich, Mateusz Putyrski, Hanh Hanuschka, Manuel Cavada, Achim Knappik, Francisco Ylera
We have shown that the displayed antibody and the anchoring SpyCatcher-pIII protein, which are translated independently of each other, form a fusion protein exclusively in the periplasm. Optimized periplasmic secretion signal peptides for each polypeptide chain can be used. In this implementation of antibody SpyDisplay, three different signal peptides are used: OmpA and PhoA for light and heavy antibody chains, and DsbA for the SpyCatcher-pIII fusion. Furthermore, we showed that the TAT pathway is compatible with SpyDisplay, enabling the cytoplasmic folding of the displayed proteins. The display rate via the TAT pathway could potentially be increased through optimization of the TAT signal peptide. We anticipate that TAT-based display will be useful for selecting intrabodies, antibodies that can fold in the cytoplasm, without the need for specialized intrabody libraries.
Biomaterial engineering surface to control polymicrobial dental implant-related infections: focusing on disease modulating factors and coatings development
Published in Expert Review of Medical Devices, 2023
Samuel S. Malheiros, Bruna E. Nagay, Martinna M. Bertolini, Erica D. de Avila, Jamil A. Shibli, João Gabriel S. Souza, Valentim A. R. Barão
Given the biological complexity of peri-implantitis and the impact of implant topography, the search for the gold-standard treatment can still be considered challenging [44,45]. In a nutshell, the treatment options can be divided into non-surgical and surgical approaches. The non-surgical procedures include the mechanical removal of biofilm from the implant surface, which can be accomplished using a wide range of methods, such as curettes [46], ultrasonic scalers [47], titanium brushes [48], air polishing devices [49], laser debridement [50] (mechanical debridement and/or photobiomodulation), often associated with local chemical adjunct treatments, such as antimicrobial photodynamic therapy [51], citric acid decontamination [52] and with local or systemic antimicrobial agents (antibiotics and chlorhexidine) [53,54]. Regardless of the approach used for non-surgical treatment of peri-implant defects [54], due to the intrabody component often found around the threads of a contaminated implant [51], surgical treatments such as resective surgery or regenerative therapy are often needed after initial phase therapy [45], but these are also still not predictable due to the difficulties in properly decontaminate the implant surface, especially when bone loss is > 50% of the total implant length [43,55]. Although intermediate results can be achieved, the literature demonstrates the need for recurrent interventions around 44% after treatment of peri-implantitis [56], and an overall low success and survival rate for implants with severe bone loss and in patients with a history of periodontitis [43,57].
Intracellular displacement of p53 using transactivation domain (p53 TAD) specific nanobodies
Published in mAbs, 2018
Anneleen Steels, Adriaan Verhelle, Olivier Zwaenepoel, Jan Gettemans
In general, antibodies are interesting tools to investigate the cellular function of proteins, because of their high affinity and specificity. However, not all antibody formats are sufficiently stable and robust in the reducing cytoplasmic environment. For example, full-length antibodies contain several inter- and intramolecular disulfide bridges, which cannot be formed in the cytoplasm resulting in their partial unfolding and loss-of-function.42 Nbs, however, display a remarkably stable behavior and can resist chemical and thermal denaturation. This makes them suitable candidates for use as an intrabody.17 The intracellular stability of our nanobody set was tested via an in vivo pull down experiment (Figure 3). The majority of the Nbs experienced no hinderance from the reducing environment and were capable of binding endogenous p53 when expressed intracellularly. p53 TAD Nb91 was, in spite of its satisfactory intracellular expression, not able to pull down p53. Its rather low affinity (~ 2.68 ± 0.69 µM) probably accounts for this observation (Figure 2(c)). Curiously, intracellular expression could not be detected for p53 TAD Nb18 and p53 TAD Nb25, resulting in a negative outcome in the in vivo pull down (Figure 3). Possibly, these two Nbs are an exception to the rule and display a low intracellular stability resulting in their unfolding.