This paper aims at understanding the First World War in the German colony of Deutsch-Ostafrika from all important perspectives. It aims to show that the situation led to a crisis of colonialism; Therefore, it firstly takes a close look at the actual history of the course of the First World War in Deutsch-Ostafrika and its immediate effects for the African population. Its arguments are that German armed forces consisted mainly of African soldiers under white officers, whose constant replacement weakened the army. A lack of supplies and infrastructure led to lootings and the forced recruitment of local porters, of whom many died in service, and whose absence on their fields let to famine. The Germans therefore were at the good will of Africans, what undermined the classical colonial distribution of roles. Until the war there had been an ideological frontier between black Africans and whites of all European nations. This was important to establish a deterring system of representation, to make Africans feel inferior and not to attempt revolt. The war changed this radically, as black soldiers learned to kill white people and to understand their weaknesses. For long, furthermore colonial missionaries had struggled to spread Christianity among natives; the waring Europeans’ display of “Christianity” though led to major setbacks. The following spiritual vacuum was in part filled by the spread of Islam. The paper argues that this interplay of military, ideological and religious points shook the colonial system to its foundations. The article’s final chapter traces how some of the events of the war in Africa then effected the subsequent period.
A family of histidine-rich peptides LAH4 was designed using linear cationic peptides such as magainins as a template. These designed peptides have been shown to exhibit considerable antimicrobial, nucleic acid transfection as well as cell penetrating activities. In contrast to their natural templates their membrane interactions are strongly pH dependent. The delivery of cargo by these peptides is complex, involving many steps, which we investigated on a structural and biophysical level. Recently, vectofusin-1, a member of the family of LAH4 peptides has been shown to spontaneously self-assemble into helical coiled-coil structures, spherical aggregates, that further assemble into annular and extended nanofibrils and hydrogels as a function of phosphate and in a pH-dependent manner. This bears considerable interest for the design of biomaterials. Furthermore, the peptide has a strong capacity to enhance the gene transfer by lenti- and adeno associated viruses into the cell interior. Thereby, the fibers formed by this short peptide have gene therapeutic applications ranging from monogenic and infectious diseases to cancer, by enhancing transduction levels of target cells and reducing the amount of lentivirus for greater safety and reduced costs. Vectofusin-1 promotes the entry of several retroviral pseudotypes into target cells when added to the culture medium, without cytotoxicity. These associate with viral particles allowing them to be easily pelleted. These fibrils have a unique coiled-coil α-helical structure whereas most other viral transduction enhancers form β-amyloid fibrils. Our observations define vectofusin-1 as a member of a new class of α-helical lentiviral transduction enhancers. Its coiled-coil fibril formation is reversible which bears considerable advantages in handling the peptide in conditions well-adapted to scalable gene therapy protocols. References: J PepSci 21, 346 (2015), JPC B 119, 9678 (2015), JBC 291, 2161 (2016), Acta Biomat (2017 in press), SciRep 7:9585 (2017).
Summary Two new Heteroptera species, Xylastodoris gerdae n. sp. and Hypsipteryx hoffeinsorum n. sp., are described from Baltic amber. It is the first record of tropical palm bugs (Thaumasto- coridae: Xylastodorinae) for the Palaearctic and for Baltic amber, and the first fossil record and first Palaearctic record for the bug family Hypsipterygidae that are now only known from the Palaeotropis.